-
1
-
-
0000489779
-
Importance of organic radicals in enzymic cleavage of unactivated carbon-hydrogen bonds
-
This is a pivotal review article highlighting aerobic and anaerobic mechanisms for the cleavage of unactivated C-H bonds. The article advances the thesis that metal ions are required to generate oxidants of sufficient potency to cleave such bonds.
-
Frey P.A. Importance of organic radicals in enzymic cleavage of unactivated carbon-hydrogen bonds. Chem Rev 90 (1990) 1343-1357. This is a pivotal review article highlighting aerobic and anaerobic mechanisms for the cleavage of unactivated C-H bonds. The article advances the thesis that metal ions are required to generate oxidants of sufficient potency to cleave such bonds.
-
(1990)
Chem Rev
, vol.90
, pp. 1343-1357
-
-
Frey, P.A.1
-
2
-
-
1542378704
-
Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates
-
Costas M., Mehn M.P., Jensen M.P., and Que Jr. L. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem Rev 104 (2004) 939-986
-
(2004)
Chem Rev
, vol.104
, pp. 939-986
-
-
Costas, M.1
Mehn, M.P.2
Jensen, M.P.3
Que Jr., L.4
-
3
-
-
0000502480
-
Isopenicillin N synthase: mechanistic studies
-
Baldwin J.E., and Bradley M. Isopenicillin N synthase: mechanistic studies. Chem Rev 90 (1990) 1079-1088
-
(1990)
Chem Rev
, vol.90
, pp. 1079-1088
-
-
Baldwin, J.E.1
Bradley, M.2
-
6
-
-
24144485937
-
Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis
-
Vaillancourt F.H., Yeh E., Vosburg D.A., O'Connor S.E., and Walsh C.T. Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis. Nature 436 (2005) 1191-1194
-
(2005)
Nature
, vol.436
, pp. 1191-1194
-
-
Vaillancourt, F.H.1
Yeh, E.2
Vosburg, D.A.3
O'Connor, S.E.4
Walsh, C.T.5
-
7
-
-
33645017788
-
Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis
-
Blasiak L.C., Vaillancourt F.H., Walsh C.T., and Drennan C.L. Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis. Nature 440 (2006) 368-371
-
(2006)
Nature
, vol.440
, pp. 368-371
-
-
Blasiak, L.C.1
Vaillancourt, F.H.2
Walsh, C.T.3
Drennan, C.L.4
-
8
-
-
33846379972
-
Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3
-
Galoníc D.P., Barr E.W., Walsh C.T., Bollinger Jr. J.M., and Krebs C. Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3. Nat Chem Biol 3 (2007) 113-116
-
(2007)
Nat Chem Biol
, vol.3
, pp. 113-116
-
-
Galoníc, D.P.1
Barr, E.W.2
Walsh, C.T.3
Bollinger Jr., J.M.4
Krebs, C.5
-
10
-
-
0018336512
-
The mechanism of adenosylcobalamin-dependent reactions
-
Babior B.M., and Krouwer J.S. The mechanism of adenosylcobalamin-dependent reactions. Crit Rev Biochem 6 (1979) 35-102
-
(1979)
Crit Rev Biochem
, vol.6
, pp. 35-102
-
-
Babior, B.M.1
Krouwer, J.S.2
-
13
-
-
0027297718
-
Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?
-
Frey P.A. Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?. FASEB J 7 (1993) 662-670
-
(1993)
FASEB J
, vol.7
, pp. 662-670
-
-
Frey, P.A.1
-
14
-
-
0038575234
-
S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin?
-
Frey P.A., and Magnusson O.T. S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin?. Chem Rev 103 (2003) 2129-2148
-
(2003)
Chem Rev
, vol.103
, pp. 2129-2148
-
-
Frey, P.A.1
Magnusson, O.T.2
-
15
-
-
0035282866
-
Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods
-
This paper is the first detailed bioinformatics study to recognize that proteins that use S-adenosylmethionine as a precursor to the 5′-deoxyadenosyl 5′-radical constitute a superfamily. It also highlights various subclasses of these enzymes.
-
Sofia H.J., Chen G., Hetzler B.G., Reyes-Spindola J.F., and Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29 (2001) 1097-1106. This paper is the first detailed bioinformatics study to recognize that proteins that use S-adenosylmethionine as a precursor to the 5′-deoxyadenosyl 5′-radical constitute a superfamily. It also highlights various subclasses of these enzymes.
-
(2001)
Nucleic Acids Res
, vol.29
, pp. 1097-1106
-
-
Sofia, H.J.1
Chen, G.2
Hetzler, B.G.3
Reyes-Spindola, J.F.4
Miller, N.E.5
-
17
-
-
13844275460
-
Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the 'radical-SAM' protein superfamily
-
Walsby C.J., Ortillo D., Yang J., Nnyepi M.R., Broderick W.E., Hoffman B.M., and Broderick J.B. Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the 'radical-SAM' protein superfamily. Inorg Chem 44 (2005) 727-741
-
(2005)
Inorg Chem
, vol.44
, pp. 727-741
-
-
Walsby, C.J.1
Ortillo, D.2
Yang, J.3
Nnyepi, M.R.4
Broderick, W.E.5
Hoffman, B.M.6
Broderick, J.B.7
-
18
-
-
0034841061
-
Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role
-
Cheek J., and Broderick J.B. Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role. J Biol Inorg Chem 6 (2001) 209-226
-
(2001)
J Biol Inorg Chem
, vol.6
, pp. 209-226
-
-
Cheek, J.1
Broderick, J.B.2
-
20
-
-
0002477071
-
Radical intermediates in the reaction of lysine 2,3-aminomutase
-
Zard S.Z. (Ed), JAI Press Inc.
-
Frey P.A., and Booker S. Radical intermediates in the reaction of lysine 2,3-aminomutase. In: Zard S.Z. (Ed). Advances in Free Radical Chemistry vol. 2 (1999), JAI Press Inc. 1-43
-
(1999)
Advances in Free Radical Chemistry
, vol.2
, pp. 1-43
-
-
Frey, P.A.1
Booker, S.2
-
21
-
-
0030036363
-
Evidence that oxidation of toluene in the denitrifying bacterium Thauera aromatica is initiated by formation of benzylsuccinate from toluene and fumarate
-
Biegert T., Fuchs G., and Heider J. Evidence that oxidation of toluene in the denitrifying bacterium Thauera aromatica is initiated by formation of benzylsuccinate from toluene and fumarate. Eur J Biochem 238 (1996) 661-668
-
(1996)
Eur J Biochem
, vol.238
, pp. 661-668
-
-
Biegert, T.1
Fuchs, G.2
Heider, J.3
-
22
-
-
0031694029
-
Initial reaction of anaerobic metabolism of alkylbenzenes in denitrifying and sulfate-reducing bacteria
-
Rabus R., and Heider J. Initial reaction of anaerobic metabolism of alkylbenzenes in denitrifying and sulfate-reducing bacteria. Arch Microbiol 170 (1998) 377-384
-
(1998)
Arch Microbiol
, vol.170
, pp. 377-384
-
-
Rabus, R.1
Heider, J.2
-
23
-
-
0035162901
-
Benzylsuccinate synthase of Azoarcus sp. strain T: cloning, sequencing, transcriptional organization, and its role in anaerobic toluene and m-xylene mineralization
-
Anchong G.R., Rodriguez A.M., and Spormann A.M. Benzylsuccinate synthase of Azoarcus sp. strain T: cloning, sequencing, transcriptional organization, and its role in anaerobic toluene and m-xylene mineralization. J Bacteriol 183 (2001) 6763-6770
-
(2001)
J Bacteriol
, vol.183
, pp. 6763-6770
-
-
Anchong, G.R.1
Rodriguez, A.M.2
Spormann, A.M.3
-
24
-
-
0031980567
-
Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism
-
Leuthner B., Leutwein C., Schulz H., Hoerth P., Haehnel W., Schiltz E., Schaegger H., and Heider J. Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism. Mol Microbiol 28 (1998) 615-628
-
(1998)
Mol Microbiol
, vol.28
, pp. 615-628
-
-
Leuthner, B.1
Leutwein, C.2
Schulz, H.3
Hoerth, P.4
Haehnel, W.5
Schiltz, E.6
Schaegger, H.7
Heider, J.8
-
25
-
-
0032814964
-
Substrate range of benzylsuccinate synthase from Azoarcus sp. strain T
-
Beller H.R., and Spormann A.M. Substrate range of benzylsuccinate synthase from Azoarcus sp. strain T. FEMS Microbiol Lett 178 (1999) 147-153
-
(1999)
FEMS Microbiol Lett
, vol.178
, pp. 147-153
-
-
Beller, H.R.1
Spormann, A.M.2
-
26
-
-
0031859610
-
Identification and analysis of genes involved in anaerobic toluene metabolism by strain T1: putative role of a glycine free radical
-
This paper describes the similarity between pyruvate formate-lyase and benzylsuccinate synthase with respect to a conserved glycyl residue and a conserved cysteinyl residue both of which are essential for turnover.
-
Coschigano P.W., Wehrman T.S., and Young L.Y. Identification and analysis of genes involved in anaerobic toluene metabolism by strain T1: putative role of a glycine free radical. Appl Environ Microbiol 64 (1998) 1650-1656. This paper describes the similarity between pyruvate formate-lyase and benzylsuccinate synthase with respect to a conserved glycyl residue and a conserved cysteinyl residue both of which are essential for turnover.
-
(1998)
Appl Environ Microbiol
, vol.64
, pp. 1650-1656
-
-
Coschigano, P.W.1
Wehrman, T.S.2
Young, L.Y.3
-
27
-
-
20944440930
-
Mechanism of benzylsuccinate synthase: stereochemistry of toluene addition to fumarate and maleate
-
This paper describes in vitro mechanistic analysis of the benzylsuccinate synthase reaction and provides information about the stereochemistry of toluene addition to fumarate.
-
Qiao C., and Marsh E.N.G. Mechanism of benzylsuccinate synthase: stereochemistry of toluene addition to fumarate and maleate. J Am Chem Soc 127 (2005) 8608-8609. This paper describes in vitro mechanistic analysis of the benzylsuccinate synthase reaction and provides information about the stereochemistry of toluene addition to fumarate.
-
(2005)
J Am Chem Soc
, vol.127
, pp. 8608-8609
-
-
Qiao, C.1
Marsh, E.N.G.2
-
28
-
-
65349129750
-
Analysis of the novel benzylsuccinate synthase reaction for anaerobic toluene activation based on structural studies of the product
-
Beller H.R., and Spormann A.M. Analysis of the novel benzylsuccinate synthase reaction for anaerobic toluene activation based on structural studies of the product. J Bacteriol 62 (1998) 1188-1196
-
(1998)
J Bacteriol
, vol.62
, pp. 1188-1196
-
-
Beller, H.R.1
Spormann, A.M.2
-
29
-
-
0034437363
-
Metabolism of alkylbenzenes, alkanes, and other hydrocarbons in anaerobic bacteria
-
This is a resourceful review describing the anaerobic metabolism of a variety of hydrocarbons.
-
Spormann A.M., and Widdel F. Metabolism of alkylbenzenes, alkanes, and other hydrocarbons in anaerobic bacteria. Biodegradation 11 (2000) 85-105. This is a resourceful review describing the anaerobic metabolism of a variety of hydrocarbons.
-
(2000)
Biodegradation
, vol.11
, pp. 85-105
-
-
Spormann, A.M.1
Widdel, F.2
-
31
-
-
0031694750
-
Growth, natural relationships, cellular fatty acids and metabolic adaptation of sulfate-reducing bacteria that utilize long-chain alkanes under anoxic conditions
-
Aeckersberg F., Rainey F.A., and Widdel F. Growth, natural relationships, cellular fatty acids and metabolic adaptation of sulfate-reducing bacteria that utilize long-chain alkanes under anoxic conditions. Arch Microbiol 170 (1998) 361-369
-
(1998)
Arch Microbiol
, vol.170
, pp. 361-369
-
-
Aeckersberg, F.1
Rainey, F.A.2
Widdel, F.3
-
32
-
-
0028667948
-
Anaerobic oxidation of hydrocarbons in crude oil by new types of sulphate-reducing bacteria
-
Reuter P., Rabus R., Wilkes H., Aeckersberg F., Rainey F.A., Jannasch H.W., and Widdel F. Anaerobic oxidation of hydrocarbons in crude oil by new types of sulphate-reducing bacteria. Nature 372 (1994) 455-458
-
(1994)
Nature
, vol.372
, pp. 455-458
-
-
Reuter, P.1
Rabus, R.2
Wilkes, H.3
Aeckersberg, F.4
Rainey, F.A.5
Jannasch, H.W.6
Widdel, F.7
-
33
-
-
0344947890
-
Isolation and characterization of a sulfate-reducing bacterium that anaerobically degrades alkanes
-
So C.M., and Young L.Y. Isolation and characterization of a sulfate-reducing bacterium that anaerobically degrades alkanes. Appl Environ Microbiol 65 (1999) 2969-2976
-
(1999)
Appl Environ Microbiol
, vol.65
, pp. 2969-2976
-
-
So, C.M.1
Young, L.Y.2
-
34
-
-
0033984068
-
Anaerobic oxidation of alkanes by newly isolated denitrifying bacteria
-
Ehrenreich P., Behrends A., Harder J., and Widdel F. Anaerobic oxidation of alkanes by newly isolated denitrifying bacteria. Arch Microbiol 173 (2000) 58-64
-
(2000)
Arch Microbiol
, vol.173
, pp. 58-64
-
-
Ehrenreich, P.1
Behrends, A.2
Harder, J.3
Widdel, F.4
-
35
-
-
0034466705
-
Anaerobic oxidation of n-dodecane by an addition reaction in a sulfate-reducing bacterial enrichment culture
-
This paper presents evidence that straight-chain alkanes are activated for anaerobic oxidation by the addition to fumarate, and hints that the system is similar to that of benzylsuccinate synthase.
-
Kropp K.G., Davidova I.A., and Suflita J.M. Anaerobic oxidation of n-dodecane by an addition reaction in a sulfate-reducing bacterial enrichment culture. Appl Environ Microbiol 66 (2000) 5393-5398. This paper presents evidence that straight-chain alkanes are activated for anaerobic oxidation by the addition to fumarate, and hints that the system is similar to that of benzylsuccinate synthase.
-
(2000)
Appl Environ Microbiol
, vol.66
, pp. 5393-5398
-
-
Kropp, K.G.1
Davidova, I.A.2
Suflita, J.M.3
-
36
-
-
0035110830
-
Anaerobic initial reaction of n-alkanes in a denitrifying bacterium: evidence for (1-methylpentyl)succinate as initial product and for involvement of an organic radical in n-hexane metabolism
-
This paper presents evidence that the first step in the degradation of n-hexane involves a radical addition to fumarate, as seen in benzylsuccinate synthase.
-
Rabus R., Wilkes H., Behrends A., Armstroff A., Fischer T., Pierik A.J., and Widdel F. Anaerobic initial reaction of n-alkanes in a denitrifying bacterium: evidence for (1-methylpentyl)succinate as initial product and for involvement of an organic radical in n-hexane metabolism. J Bacteriol 183 (2001) 1707-1715. This paper presents evidence that the first step in the degradation of n-hexane involves a radical addition to fumarate, as seen in benzylsuccinate synthase.
-
(2001)
J Bacteriol
, vol.183
, pp. 1707-1715
-
-
Rabus, R.1
Wilkes, H.2
Behrends, A.3
Armstroff, A.4
Fischer, T.5
Pierik, A.J.6
Widdel, F.7
-
37
-
-
38049101111
-
Genes encoding the candidate enzyme for anaerobic activation of n-alkanes in the denitrifying bacterium, strain HxN1
-
This paper describes the identification of a gene cluster that encodes proteins involved in the anaerobic activation of n-alkanes. The proteins were found to be similar to those in the benzylsuccinate synthase system.
-
Grundmann O., Behrends A., Rabus R., Amann J., Halder T., Heider J., and Widdel F. Genes encoding the candidate enzyme for anaerobic activation of n-alkanes in the denitrifying bacterium, strain HxN1. Environ Microbiol 10 (2008) 376-385. This paper describes the identification of a gene cluster that encodes proteins involved in the anaerobic activation of n-alkanes. The proteins were found to be similar to those in the benzylsuccinate synthase system.
-
(2008)
Environ Microbiol
, vol.10
, pp. 376-385
-
-
Grundmann, O.1
Behrends, A.2
Rabus, R.3
Amann, J.4
Halder, T.5
Heider, J.6
Widdel, F.7
-
38
-
-
37349050646
-
Anaerobic alkane-degrading strain AK-01 contains two alkylsuccinate synthase genes
-
This paper describes the identification of two gene clusters involved in the anaerobic activation of n-hexadecane. The encoded proteins were found to be similar to those in the benzylsuccinate synthase system.
-
Callaghan A.V., Wawrik B., Chadhain S.M.N., Young L.Y., and Zylstra G.J. Anaerobic alkane-degrading strain AK-01 contains two alkylsuccinate synthase genes. Biochem Biophys Res Commun 366 (2008) 142-148. This paper describes the identification of two gene clusters involved in the anaerobic activation of n-hexadecane. The encoded proteins were found to be similar to those in the benzylsuccinate synthase system.
-
(2008)
Biochem Biophys Res Commun
, vol.366
, pp. 142-148
-
-
Callaghan, A.V.1
Wawrik, B.2
Chadhain, S.M.N.3
Young, L.Y.4
Zylstra, G.J.5
-
39
-
-
0030175259
-
Oxidative damage to the glycyl α-carbon site in proteins: an ab initio study of the C-H bond dissociation energy and the reduction potential of the C-centered radical
-
Armstrong D.A., Yu D., and Rauk A. Oxidative damage to the glycyl α-carbon site in proteins: an ab initio study of the C-H bond dissociation energy and the reduction potential of the C-centered radical. Can J Chem 74 (1996) 1192-1199
-
(1996)
Can J Chem
, vol.74
, pp. 1192-1199
-
-
Armstrong, D.A.1
Yu, D.2
Rauk, A.3
-
40
-
-
0000906512
-
Hydrocarbon bond dissociation energies
-
McMillen D.F., and Golden D.M. Hydrocarbon bond dissociation energies. Ann Rev Phys Chem 33 (1982) 493-532
-
(1982)
Ann Rev Phys Chem
, vol.33
, pp. 493-532
-
-
McMillen, D.F.1
Golden, D.M.2
-
41
-
-
33847635732
-
S-Adenosylmethionine as an oxidant: the radical SAM superfamily
-
Wang S.C., and Frey P.A. S-Adenosylmethionine as an oxidant: the radical SAM superfamily. Trends Biochem Sci 32 (2007) 101-110
-
(2007)
Trends Biochem Sci
, vol.32
, pp. 101-110
-
-
Wang, S.C.1
Frey, P.A.2
-
42
-
-
0028280411
-
Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product
-
Sanyal I., Cohen G., and Flint D.H. Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry 33 (1994) 3625-3631
-
(1994)
Biochemistry
, vol.33
, pp. 3625-3631
-
-
Sanyal, I.1
Cohen, G.2
Flint, D.H.3
-
43
-
-
0033594329
-
Biotin synthase mechanism: evidence for hydrogen transfer from the substrate into deoxyadenosine
-
Escalettes F., Florentin D., Tse Sum Bui B., Lesage D., and Marquet A. Biotin synthase mechanism: evidence for hydrogen transfer from the substrate into deoxyadenosine. J Am Chem Soc 121 (1999) 3571-3578
-
(1999)
J Am Chem Soc
, vol.121
, pp. 3571-3578
-
-
Escalettes, F.1
Florentin, D.2
Tse Sum Bui, B.3
Lesage, D.4
Marquet, A.5
-
44
-
-
0031577321
-
Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical
-
Guianvarc'h D., Florentin D., Bui B.T.S., Nunzi F., and Marquet A. Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical. Biochem Biophys Res Commun 236 (1997) 402-406
-
(1997)
Biochem Biophys Res Commun
, vol.236
, pp. 402-406
-
-
Guianvarc'h, D.1
Florentin, D.2
Bui, B.T.S.3
Nunzi, F.4
Marquet, A.5
-
45
-
-
50849090609
-
9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase
-
Taylor A.M., Farrar C.E., and Jarrett J.T. 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase. Biochemistry 47 (2008) 9309-9317
-
(2008)
Biochemistry
, vol.47
, pp. 9309-9317
-
-
Taylor, A.M.1
Farrar, C.E.2
Jarrett, J.T.3
-
46
-
-
11144281247
-
Further investigation on the turnover of Escherichia coli biotin synthase with dethiobiotin and 9-mercaptodethiobiotin as substrates
-
Tse Sum Bui B., Lotierzo M., Escalettes F., Florentin D., and Marquet A. Further investigation on the turnover of Escherichia coli biotin synthase with dethiobiotin and 9-mercaptodethiobiotin as substrates. Biochemistry 43 (2004) 16432-16441
-
(2004)
Biochemistry
, vol.43
, pp. 16432-16441
-
-
Tse Sum Bui, B.1
Lotierzo, M.2
Escalettes, F.3
Florentin, D.4
Marquet, A.5
-
48
-
-
0032573608
-
Biotin synthase mechanism: on the origin of sulphur
-
Tse Sum Bui B., Florentin B., Fournier F., Ploux O., Méjean A., and Marquet A. Biotin synthase mechanism: on the origin of sulphur. FEBS Lett 440 (1998) 226-230
-
(1998)
FEBS Lett
, vol.440
, pp. 226-230
-
-
Tse Sum Bui, B.1
Florentin, B.2
Fournier, F.3
Ploux, O.4
Méjean, A.5
Marquet, A.6
-
49
-
-
1242285458
-
Characterization of the cofactor composition of Escherichia coli biotin synthase
-
Cosper M.M., Jameson G.N.L., Hernández H.L., Krebs C., Huynh B.H., and Johnson M.K. Characterization of the cofactor composition of Escherichia coli biotin synthase. Biochemistry 43 (2004) 2007-2021
-
(2004)
Biochemistry
, vol.43
, pp. 2007-2021
-
-
Cosper, M.M.1
Jameson, G.N.L.2
Hernández, H.L.3
Krebs, C.4
Huynh, B.H.5
Johnson, M.K.6
-
50
-
-
0035902569
-
Biotin synthase contains two distinct iron-sulfur binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
-
Ugulava N.B., Gibney B.R., and Jarrett J.T. Biotin synthase contains two distinct iron-sulfur binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Biochemistry 40 (2001) 8343-8351
-
(2001)
Biochemistry
, vol.40
, pp. 8343-8351
-
-
Ugulava, N.B.1
Gibney, B.R.2
Jarrett, J.T.3
-
52
-
-
33645228923
-
2+ cluster in the sulfur insertion step
-
This paper describes a study in which a spectroscopically characterized [2Fe-2Se] cluster on biotin synthase was shown to give rise to selenobiotin, supporting the hypothesis that the [2Fe-2S] cluster is the sulfur donor in the biotin synthase reaction.
-
2+ cluster in the sulfur insertion step. Biochemistry 45 (2006) 3824-3834. This paper describes a study in which a spectroscopically characterized [2Fe-2Se] cluster on biotin synthase was shown to give rise to selenobiotin, supporting the hypothesis that the [2Fe-2S] cluster is the sulfur donor in the biotin synthase reaction.
-
(2006)
Biochemistry
, vol.45
, pp. 3824-3834
-
-
Tse Sum Bui, B.1
Mattioli, T.A.2
Florentin, D.3
Bolbach, G.4
Marquet, A.5
-
53
-
-
0035902555
-
Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion
-
This paper provides the first evidence that the active form of biotin synthase contains both a [2Fe-2S] cluster and a [4Fe-4S] cluster, and that sulfur in biotin derives from the [2Fe-2S] cluster.
-
Ugulava N.B., Sacanell C.J., and Jarrett J.T. Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion. Biochemistry 40 (2001) 8352-8358. This paper provides the first evidence that the active form of biotin synthase contains both a [2Fe-2S] cluster and a [4Fe-4S] cluster, and that sulfur in biotin derives from the [2Fe-2S] cluster.
-
(2001)
Biochemistry
, vol.40
, pp. 8352-8358
-
-
Ugulava, N.B.1
Sacanell, C.J.2
Jarrett, J.T.3
-
54
-
-
1242330269
-
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase
-
This paper describes the use of rapid kinetics methods coupled with Mössbauer, EPR, and UV-vis spectroscopies to show that the [2Fe-2S] cluster decays faster than biotin is produced. It highlights the need to apply these kinds of physical methods to peer deeply into the mechanism of radical SAM proteins.
-
Jameson G.N.L., Cosper M.M., Hernández H.L., Johnson M.K., and Huynh B.H. Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase. Biochemistry 43 (2004) 2022-2031. This paper describes the use of rapid kinetics methods coupled with Mössbauer, EPR, and UV-vis spectroscopies to show that the [2Fe-2S] cluster decays faster than biotin is produced. It highlights the need to apply these kinds of physical methods to peer deeply into the mechanism of radical SAM proteins.
-
(2004)
Biochemistry
, vol.43
, pp. 2022-2031
-
-
Jameson, G.N.L.1
Cosper, M.M.2
Hernández, H.L.3
Johnson, M.K.4
Huynh, B.H.5
-
55
-
-
0346727529
-
Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
-
This paper describes the X-ray structure of biotin synthase. All substrates and cofactors are bound, allowing a glimpse at the arrangement of the active site of an enzyme that catalyzes sulfur insertion.
-
Berkovitch F., Nicolet Y., Wan J.T., Jarrett J.T., and Drennan C.L. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303 (2004) 76-79. This paper describes the X-ray structure of biotin synthase. All substrates and cofactors are bound, allowing a glimpse at the arrangement of the active site of an enzyme that catalyzes sulfur insertion.
-
(2004)
Science
, vol.303
, pp. 76-79
-
-
Berkovitch, F.1
Nicolet, Y.2
Wan, J.T.3
Jarrett, J.T.4
Drennan, C.L.5
-
56
-
-
35348854977
-
Self-sacrifice in radical S-adenosylmethionine proteins
-
This review article compares and contrasts radical SAM proteins that catalyze sulfur-insertion reactions.
-
Booker S.J., Cicchillo R.M., and Grove T.L. Self-sacrifice in radical S-adenosylmethionine proteins. Curr Opin Chem Biol 11 (2007) 543-552. This review article compares and contrasts radical SAM proteins that catalyze sulfur-insertion reactions.
-
(2007)
Curr Opin Chem Biol
, vol.11
, pp. 543-552
-
-
Booker, S.J.1
Cicchillo, R.M.2
Grove, T.L.3
-
57
-
-
17844383968
-
Biotin synthase is catalytic in vivo, but catalysis engenders destruction of the protein
-
Choi-Rhee E., and Cronan J.E. Biotin synthase is catalytic in vivo, but catalysis engenders destruction of the protein. Chem Biol 12 (2005) 461-468
-
(2005)
Chem Biol
, vol.12
, pp. 461-468
-
-
Choi-Rhee, E.1
Cronan, J.E.2
-
58
-
-
33947624626
-
The iron-sulfur proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae
-
Mühlenhoff U., Gerl M.J., Flauger B., Pirner H.M., Balser S., Richardt N., Lill R., and Stolz J. The iron-sulfur proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae. Eukaryot Cell 6 (2007) 495-504
-
(2007)
Eukaryot Cell
, vol.6
, pp. 495-504
-
-
Mühlenhoff, U.1
Gerl, M.J.2
Flauger, B.3
Pirner, H.M.4
Balser, S.5
Richardt, N.6
Lill, R.7
Stolz, J.8
-
59
-
-
9144220291
-
MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA
-
Pierrel F., Douki T., Fontecave M., and Atta M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J Biol Chem 279 (2004) 47555-47653
-
(2004)
J Biol Chem
, vol.279
, pp. 47555-47653
-
-
Pierrel, F.1
Douki, T.2
Fontecave, M.3
Atta, M.4
-
60
-
-
40849111520
-
RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli
-
Anton B.P., Saleh L., Benner J.S., Raleigh E.A., Kasif S., and Roberts R.J. RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli. Proc Natl Acad Sci U S A 105 (2008) 1826-1831
-
(2008)
Proc Natl Acad Sci U S A
, vol.105
, pp. 1826-1831
-
-
Anton, B.P.1
Saleh, L.2
Benner, J.S.3
Raleigh, E.A.4
Kasif, S.5
Roberts, R.J.6
-
61
-
-
0033608079
-
C-H and N-H bond dissociation energies of small aromatic hydrocarbons
-
Barckholtz C., Barckholtz T.A., and Hadad C.M. C-H and N-H bond dissociation energies of small aromatic hydrocarbons. J Am Chem Soc 121 (1999) 491-500
-
(1999)
J Am Chem Soc
, vol.121
, pp. 491-500
-
-
Barckholtz, C.1
Barckholtz, T.A.2
Hadad, C.M.3
-
62
-
-
33846025127
-
Dynamic regulation of histone lysine methylation by demethylases
-
Shi Y., and Whetstine J.R. Dynamic regulation of histone lysine methylation by demethylases. Mol Cell 25 (2007) 1-14
-
(2007)
Mol Cell
, vol.25
, pp. 1-14
-
-
Shi, Y.1
Whetstine, J.R.2
-
63
-
-
0036495007
-
A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?
-
Chinenov Y. A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?. Trends Biochem Sci 27 (2002) 115-117
-
(2002)
Trends Biochem Sci
, vol.27
, pp. 115-117
-
-
Chinenov, Y.1
-
64
-
-
0033213404
-
Bioactive natural products with carbon-phosphorus bonds and their biosynthesis
-
Seto H., and Kuzuyama T. Bioactive natural products with carbon-phosphorus bonds and their biosynthesis. Nat Prod Rep 16 (1999) 589-596
-
(1999)
Nat Prod Rep
, vol.16
, pp. 589-596
-
-
Seto, H.1
Kuzuyama, T.2
-
65
-
-
33845955006
-
Rings, radicals, and regeneration: the early years of a bioorganic laboratory
-
van der Donk W.A. Rings, radicals, and regeneration: the early years of a bioorganic laboratory. J Org Chem 71 (2006) 9561-9571
-
(2006)
J Org Chem
, vol.71
, pp. 9561-9571
-
-
van der Donk, W.A.1
-
66
-
-
0028858189
-
Nucleotide sequence of fortimicin KL1 methyltransferase gene isolated from Micromonospora olivasterospora, and comparison of its deduced amino acid sequence with those of methyltransferases involved in the biosynthesis of bialaphos and fosfomycin
-
This paper provides bioinformatics evidence that radical SAM-dependent P-methylation and C-methylation might be catalyzed via similar mechanisms.
-
Kuzuyama T., Seki T., Dairi T., Hidaka T., and Seto H. Nucleotide sequence of fortimicin KL1 methyltransferase gene isolated from Micromonospora olivasterospora, and comparison of its deduced amino acid sequence with those of methyltransferases involved in the biosynthesis of bialaphos and fosfomycin. J Antibiot 48 (1995) 1191-1193. This paper provides bioinformatics evidence that radical SAM-dependent P-methylation and C-methylation might be catalyzed via similar mechanisms.
-
(1995)
J Antibiot
, vol.48
, pp. 1191-1193
-
-
Kuzuyama, T.1
Seki, T.2
Dairi, T.3
Hidaka, T.4
Seto, H.5
-
67
-
-
0026724852
-
Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme
-
This interesting paper provides compelling evidence that methylcobalamin serves as the methyl donor in P-methylases.
-
Kamigiri K., Hidaka T., Imai S., Murakami T., and Seto H. Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme. J Antibiot 45 (1992) 781-787. This interesting paper provides compelling evidence that methylcobalamin serves as the methyl donor in P-methylases.
-
(1992)
J Antibiot
, vol.45
, pp. 781-787
-
-
Kamigiri, K.1
Hidaka, T.2
Imai, S.3
Murakami, T.4
Seto, H.5
-
68
-
-
0040735636
-
Methylcorrinoids methylate radicals - their second biological mode of action
-
Mosimann H., and Kräutler B. Methylcorrinoids methylate radicals - their second biological mode of action. Angew Chem Int Ed 39 (2000) 393-395
-
(2000)
Angew Chem Int Ed
, vol.39
, pp. 393-395
-
-
Mosimann, H.1
Kräutler, B.2
-
69
-
-
34548512297
-
Chlorophyll biosynthesis in bacteria: the origins of structural and functional diversity
-
This is an interesting review article on chlorophyll biosynthesis in bacteria. It mentions several steps that potentially involve novel radical SAM chemistry, including C-methylation, oxygenation, and anaerobic oxidative cyclization.
-
Gomez Macqueo Chew A., and Bryant D.A. Chlorophyll biosynthesis in bacteria: the origins of structural and functional diversity. Ann Rev Microbiol 61 (2007) 113-129. This is an interesting review article on chlorophyll biosynthesis in bacteria. It mentions several steps that potentially involve novel radical SAM chemistry, including C-methylation, oxygenation, and anaerobic oxidative cyclization.
-
(2007)
Ann Rev Microbiol
, vol.61
, pp. 113-129
-
-
Gomez Macqueo Chew, A.1
Bryant, D.A.2
-
70
-
-
33846418769
-
Recent advances in chlorophyll biosynthesis
-
Bollivar D.W. Recent advances in chlorophyll biosynthesis. Photosynth Res 90 (2006) 173-194
-
(2006)
Photosynth Res
, vol.90
, pp. 173-194
-
-
Bollivar, D.W.1
-
71
-
-
0034612350
-
Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor
-
This is a pivotal paper reporting the requirement of cobalamin in the anaerobic oxidative cyclization reaction in chlorophyll biosynthesis.
-
Gough S.P., Petersen B.O., and Duus J.Ø. Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor. Proc Natl Acad Sci U S A 97 (2000) 6908-6913. This is a pivotal paper reporting the requirement of cobalamin in the anaerobic oxidative cyclization reaction in chlorophyll biosynthesis.
-
(2000)
Proc Natl Acad Sci U S A
, vol.97
, pp. 6908-6913
-
-
Gough, S.P.1
Petersen, B.O.2
Duus, J.Ø.3
-
72
-
-
33847294773
-
Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12
-
Gray M.J., and Escalante-Semerena J.C. Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12. Proc Natl Acad Sci U S A 104 (2007) 2921-2926
-
(2007)
Proc Natl Acad Sci U S A
, vol.104
, pp. 2921-2926
-
-
Gray, M.J.1
Escalante-Semerena, J.C.2
-
73
-
-
51949095627
-
Anaerobic oxidation of methane: mechanisms, bioenergetics, and the ecology of associated microoganisms
-
Caldwell S.L., Laidler J.R., Brewer E.A., Eberly J.O., Sandborgh S.C., and Colwell F.S. Anaerobic oxidation of methane: mechanisms, bioenergetics, and the ecology of associated microoganisms. Environ Sci Technol 42 (2008) 6791-6799
-
(2008)
Environ Sci Technol
, vol.42
, pp. 6791-6799
-
-
Caldwell, S.L.1
Laidler, J.R.2
Brewer, E.A.3
Eberly, J.O.4
Sandborgh, S.C.5
Colwell, F.S.6
-
74
-
-
4444370893
-
Reverse methanogenesis: testing the hypothesis with environmental genomics
-
Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D., Richardson P.M., and DeLong E.F. Reverse methanogenesis: testing the hypothesis with environmental genomics. Science 305 (2004) 1457-1462
-
(2004)
Science
, vol.305
, pp. 1457-1462
-
-
Hallam, S.J.1
Putnam, N.2
Preston, C.M.3
Detter, J.C.4
Rokhsar, D.5
Richardson, P.M.6
DeLong, E.F.7
-
75
-
-
9144257242
-
A conspicuous nickel protein in microbial mats that oxidize methane anaerobically
-
This is an interesting paper, which advances the thesis that the oxidation of methane might be catalyzed by a nickel-containing protein in a reaction that is predicted to be the reverse of methyl-coenzyme M reductase.
-
Krüger M., Meyerdierks A., Glöckner F.O., Amann R., Widdel F., Kube M., Reinhardt R., Kahnt J., Böcher R., Thauer R.K., et al. A conspicuous nickel protein in microbial mats that oxidize methane anaerobically. Nature 426 (2003) 878-881. This is an interesting paper, which advances the thesis that the oxidation of methane might be catalyzed by a nickel-containing protein in a reaction that is predicted to be the reverse of methyl-coenzyme M reductase.
-
(2003)
Nature
, vol.426
, pp. 878-881
-
-
Krüger, M.1
Meyerdierks, A.2
Glöckner, F.O.3
Amann, R.4
Widdel, F.5
Kube, M.6
Reinhardt, R.7
Kahnt, J.8
Böcher, R.9
Thauer, R.K.10
-
76
-
-
33645876469
-
A microbial consortium couples anaerobic methane oxidation to denitrification
-
Raghoebarsing A.A., Pol A., van de Pas-Schoonen K.T., Smolders A.J., Ettwig K.F., Rijpstra W.I., Schouten S., Damsté J.S., Op den Camp H.J., Jetten M.S., et al. A microbial consortium couples anaerobic methane oxidation to denitrification. Nature 440 (2006) 918-921
-
(2006)
Nature
, vol.440
, pp. 918-921
-
-
Raghoebarsing, A.A.1
Pol, A.2
van de Pas-Schoonen, K.T.3
Smolders, A.J.4
Ettwig, K.F.5
Rijpstra, W.I.6
Schouten, S.7
Damsté, J.S.8
Op den Camp, H.J.9
Jetten, M.S.10
|