Rhodobacter capsulatus magnesium chelatase subunit BchH contains an oxygen sensitive iron-sulfur cluster

Archives of Microbiology

Volumn 188, Issue 6, 2007, Pages 599-608

  Sirijovski, Nick ^a   Mamedov, Fikret ^b   Olsson, Ulf ^a   Styring, Stenbjörn ^b   Hansson, Mats ^a  

^a LUND UNIVERSITY   (Sweden)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Bacteriochlorophyll; chlH; Chlorophyll; Enzyme: Magnesium chelatase EC 6.6.1.1; Tetrapyrrole; Xantha f

Indexed keywords

AMINOLEVULINIC ACID; BACTERIOCHLOROPHYLL; CYSTEINE; ENZYME; IRON SULFUR PROTEIN; MAGNESIUM CHELATASE; OXYGEN; PROTEIN BCHH; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL CELL; BACTERIAL METABOLISM; BACTERIAL STRAIN; BIOSYNTHESIS; CELL CULTURE; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME SUBUNIT; NONHUMAN; OXYGEN SENSING; PHOTOSENSITIZATION; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PROTEOBACTERIA; RHODOBACTER CAPSULATUS; RHODOSPIRILLACEAE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SUBSTITUTION REACTION; ULTRAVIOLET SPECTROSCOPY;

AMINO ACID MOTIFS; BACTERIOCHLOROPHYLLS; CYSTEINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; IRON-SULFUR PROTEINS; LYASES; OXYGEN; RHODOBACTER CAPSULATUS; SPECTRUM ANALYSIS;

PROTEOBACTERIA; RHODOBACTER CAPSULATUS;

EID: 36849009712     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-007-0282-1     Document Type: Article

References (47)

1. Agarwalla S, Stroud RM, Gaffney BJ (2004) Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies. J Biol Chem 279:34123-34129
2. Axelsson E, Lundqvist J, Sawicki A, Nilsson S, Schröder I, Al-Karadaghi S, Willows RD, Hansson M (2006) Recessiveness and dominance in barley mutants deficient in Mg-chelatase subunit D, an AAA protein involved in chlorophyll biosynthesis. Plant Cell 18:3606-3616
3. Bauer CE, Bird TH (1996) Regulatory circuits controlling photosynthesis gene expression. Cell 85:5-8
4. Beinert H, Holm RH, Munck E (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277:653-659
5. Beinert H, Kennedy MC, Stout CD (1996) Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein. Chem Rev 96:2335-2374
6. Beja O, Suzuki MT, Heidelberg JF, Nelson WC, Preston CM, Hamada T, Eisen JA, Fraser CM, DeLong EF (2002) Unsuspected diversity among marine aerobic anoxygenic phototrophs. Nature 415:630-633
7. Biel AJ (1992) Oxygen-regulated steps in the Rhodobacter capsulatus tetrapyrrole biosynthetic pathway. J Bacteriol 174:5272-5274
8. Biel AJ, Marrs BM (1983) Transcriptional regulation of several genes for bacteriochlorophyll biosynthesis in Rhodopseudomonas capsulatus in response to oxygen. J Bacteriol 156:686-694
9. 420-reducing hydrogenase of Methanococcus voltae. Eur J Biochem 267:6612-6618
10. Bollivar DW, Suzuki JY, Beatty JT, Dobrowolski JM, Bauer CE (1994) Directed mutational analysis of bacteriochlorophyll a biosynthesis in Rhodobacter capsulatus. J Mol Biol 237:622-640
11. Brown NM, Kennedy MC, Antholine WE, Eisenstein RS, Walden WE (2002) Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1. Insights into the mechanism of Fe-S cluster cycling. J Biol Chem 277:7246-7254
12. Cammack R (1992) Iron-sulfur clusters in enzymes: themes and variations. Adv Inorg Chem 38:281-322
13. Cohen-Bazire G, Sistrom WR, Stanier RY (1957) Kinetic studies of pigment synthesis by non-sulfur purple bacteria. J Cell Physiol 49:25-68
14. Conover RC, Kowal AT, Fu WG, Park JB, Aono S, Adams MW, Johnson MK (1990) Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin. J Biol Chem 265:8533-8541
15. Coomber SA, Chaudhri M, Connor A, Britton G, Hunter CN (1990) Localized transposon Tn5 mutagenesis of the photosynthetic gene cluster of Rhodobacter sphaeroides. Mol Microbiol 4:977-989
16. Cunningham RP, Asahara H, Bank JF, Scholes CP, Salerno JC, Surerus K, Munck E, McCracken J, Peisach J, Emptage MH (1989) Endonuclease III is an iron-sulfur protein. Biochemistry 28:4450-4455
17. Dailey HA, Finnegan MG, Johnson MK (1994) Human ferrochelatase is an iron-sulfur protein. Biochemistry 33:403-407
18. Dailey TA, Dailey HA (2002) Identification of [2Fe-2S] clusters in microbial ferrochelatases. J Bacteriol 184:2460-2464
19. Falk JE (1964) Porphyrins and metalloporphyrins. Elsevier Publishing Company, Amsterdam
20. Ferreira G, Franco R, Lloyd S, Pereira A, Moura I, Moura J, Huynh B (1994) Mammalian ferrochelatase, a new addition to the metalloenzyme family. J Biol Chem 269:7062-7065
21. Fling SP, Gregerson DS (1986) Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea. Anal Biochem 155:83-88
22. Fodje MN, Hansson A, Hansson M, Olsen JG, Gough S, Willows RD, Al-Karadaghi S (2001) Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase. J Mol Biol 311:111-122
23. Gibson LCD, Willows RD, Kannanagara CG, von Wettstein D, Hunter CN (1995) Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitution of activity by combining the products of the bchH, -I, and -D genes expressed in Escherichia coli. Proc Natl Acad Sci USA 92:1941-1944
24. Gorchein A (1973) Control of magnesium protoporphyrin chelatase activity in Rhodopsedomonas spheroides. Biochem J 134:833-845
25. Guigliarelli B, Bertrand P (1999) Application of EPR spectroscopy to the structural and functional study of iron-sulfur proteins. Adv Inorg Chem 47:421-497
26. Higgins D, Thompson J, Gibson T, Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting,position-specific gap penalties and weight matrix choice. Nucl Acids Res 22:4673-4680
27. Hinks JA, Evans MCW, de Miguel Y, Sartori AA, Jiricny J, Pearl LH (2002) An iron-sulfur cluster in the family 4 uracil-DNA glycosylases. J Biol Chem 277:16936-16940
28. Hägerhäll C, Sled V, Hederstedt L, Ohnishi T (1995) The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties. Biochim Biophys Acta 1129:356-362
29. L: evidence for a 4Fe-4S center housed within an MXCXXC motif. J Biol Chem 278:41900-41907
30. + clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activase in vitro. J Biol Chem 275:12367-12373
31. Madigan MT, Gest H (1978) Growth of a photosynthetic bacterium anaerobically in darkness, supported by "oxidant-dependent" sugar fermentation. Arch Microbiol 117:119-122
32. 2 as the energy source. J Bacteriol 137:524-530
33. Mandori A, Cecchini G, Schröder I, Gunsalus RP, Werth MT, Johnson MK (1992) [3Fe-S] to [4Fe-S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis. Biochemistry 31:2703-2712
34. Morgan TV, Stephens PJ, Devlin F, Burgess BK, Stout CD (1985) Selective oxidative destruction of iron-sulfur clusters. Ferricyanide oxidation of Azotobacter vinelandii ferredoxin I. FEBS Lett 183:206-210
35. 27C) in the Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8. J Biol Chem 277:1680-1688
36. Neuhoff V, Arold N, Taube D, Ehrhardt W (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9:255-262
37. Ouchane S, Steunou A, Picaud M, Astier C (2004) Aerobic and anaerobic Mg-protoporphyrin monomethyl ester cyclases in purple bacteria. J Biol Chem 279:6385-6394
38. Pinta V, Picaud M, Reiss-Husson F, Astier C (2002) Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron- cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester. J Bacteriol 184:746-753
39. Raux-Deery E, Leech HK, Nakrieko K-A, McLean KJ, Munro AW, Heathcote P, Rigby SEJ, Smith AG, Warren MJ (2005) Identification and characterization of the terminal enzyme of siroheme biosynthesis from Arabidopsis thaliana: a plastid-located sirohydrochlorin ferrochelatase containing a 2Fe-2S center. J Biol Chem 280:4713-4721
40. Rothery RA, Weiner JH (1993) Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster. Biochemistry 32:5855-5861
41. Swingley WD, Sadekar S, Mastrian SD, Matthies HJ, Hao J, Ramos H, Acharya CR, Conrad AL, Taylor HL, Dejesa LC, Shah MK, O'Huallachain M E, Lince MT, Blankenship RE, Beatty JT, Touchman JW (2007) The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism. J Bacteriol 189:683-690
42. Waidner LA, Kirchman DL (2005) Aerobic anoxygenic photosynthesis genes and operons in uncultured bacteria in the Delaware River. Environ Micro 7:1896-1908
43. Willows RD, Beale SI (1998) Heterologous expression of the Rhodobacter capsulatus BchI, -D, and -H genes that encode magnesium chelatase subunits and characterization of the reconstituted enzyme. J Biol Chem 273:34206-34213
44. Willows RD, Gibson LCD, Kanangara CG, Hunter CN, von Wettstein D (1996) Three separate proteins constitute the magnesium chelatase of Rhodobacter sphaeroides. Eur J Biochem 235:438-443
45. Willows RD, Hansson M (2003) Mechanism, structure, and regulation of magnesium chelatase. In: Kadish KM, Smith KM, Guildard R (eds) The tetrapyrrole handbook II. Academic, New York, pp 1-48
46. Willows RD, Lake V, Roberts TH, Beale SI (2003) Inactivation of Mg chelatase during transition from anaerobic to aerobic growth in Rhodobacter capsulatus. J Bacteriol 185:3249-3258
47. Yano T, Yagi T, Sled VD, Ohnishi T (1995) Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J Biol Chem 270:18264-18270