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Metallocenter assembly in nickel-containing enzymes
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Hausinger RP: Metallocenter assembly in nickel-containing enzymes. J Biol Inorg Chem 1997, 2:279-286. This review discusses the pathways of Ni-cofactor assembly for Ni enzymes.
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J Biol Inorg Chem
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Hausinger, R.P.1
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0030612325
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The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase
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Olson JW, Fu CL, Maier RJ: The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase. Mol Microbiol 1997, 24:119-128. This manuscript describes a novel function for a protein that is probably present in all systems involved in assembling Ni cofactors. The authors took advantage of some unique aspects of B. japonicum to support the hypothesis that HypB plays an important role when organisms are subjected a low-Ni milieu.
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Mol Microbiol
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Olson, J.W.1
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A novel nickel-containing superoxide dismutase from Streptomyces spp
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Youn H-D, Kim E-J, Roe J-H, Hah YC, Kang S-O: A novel nickel-containing superoxide dismutase from Streptomyces spp. Biochem J 1996, 318:889-896.
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0029849183
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Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor
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Kim EJ, Kim HP, Hah YC, Roe JH: Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor. Eur J Biochem 1996, 241:178-185.
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Eur J Biochem
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Kim, E.J.1
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Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller
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Kim E-J, Chung H-J, Suh B, Hah YC, Roe J-H: Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller. Mol Microbiol 1998, 27:187-195.
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Kim, E.-J.1
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9
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0030588257
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Unique isozymes of superoxide dismutase in Streptomyces griseus
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Youn H-D, Youn H, Lee J-W, Yim Y-I, Lee JK, Hah YC, Kang S-O: Unique isozymes of superoxide dismutase in Streptomyces griseus. Arch Biochem Biophys 1996, 334:341-348. This paper describes properties of the novel Ni-SOD.
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Arch Biochem Biophys
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Youn, H.-D.1
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Kang, S.-O.7
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11
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0001849211
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70 years of crystalline urease: What have we learned?
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Karplus PA, Pearson MA, Hausinger RP: 70 years of crystalline urease: what have we learned? Accounts Chem Res 1997, 30:330-337. This is an authoritative review of the structure and mechanism of urease and is a must read for following this field.
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Accounts Chem Res
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Karplus, P.A.1
Ma, P.2
Hausinger, R.P.3
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12
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0029647957
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The crystal structure of urease from Klebsiella aerogenes
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Jabri E, Carr MB, Hausinger RP, Karplus PA: The crystal structure of urease from Klebsiella aerogenes. Science 1995, 268:998-1004.
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Science
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Jabri, E.1
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13
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0030848288
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Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease
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Pearson MA, Michel LO, Hausinger RP, Karplus PA: Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease. Biochemistry 1997, 36:8164-8172. This paper refines the structure of urease which, to a large extent, forms the basis for the proposed catalytic mechanism.
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Biochemistry
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Ma, P.1
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0001872664
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Urease nickel metallocenter: Structure and assembly
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Taha RSM, Brayman TG, Karplus PA, Hausinger RP: Urease nickel metallocenter: structure and assembly. In Transition metals in microbial metabolism. Edited by Winkelmann G, Carrano CJ. Amsterdam: Harwood Academic Publishers; 1997:391-413.
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Transition Metals in Microbial Metabolism
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Rsm, T.1
Brayman, T.G.2
Karplus, P.A.3
Hausinger, R.P.4
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15
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0030725701
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Substitution of the urease active site carbamate by dithiocarbamate and vanadate
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Yamaguchi K, Hausinger RP: Substitution of the urease active site carbamate by dithiocarbamate and vanadate. Biochemistry 1997, 36:15118-15122.
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Biochemistry
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Yamaguchi, K.1
Hausinger, R.P.2
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0030873130
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Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide- Binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease
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Moncrief MBC, Hausinger RP: Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide- binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease. J Bacteriol 1997, 179:4081-4086.
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J Bacteriol
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Mbc, M.1
Hausinger, R.P.2
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0029809744
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Purification and activation properties of UreD-UreF-urease apoprotein
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Moncrief MBC, Hausinger RP: Purification and activation properties of UreD-UreF-urease apoprotein. J Bacteriol 1996, 178:5417-5421.
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J Bacteriol
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Mbc, M.1
Hausinger, R.P.2
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0029848538
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Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA)
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Kansau I, Guillain F, Thiberge JM, Labigne A: Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA). Mol Microbiol 1996, 22:1013-1023.
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Mol Microbiol
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Kansau, I.1
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0029869181
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Purification, properties and primary structure of H2- Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus
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Hartmann GC, Klein AR, Linder M, Thauer RK: Purification, properties and primary structure of H2- forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus. Arch Microbiol 1996, 165:187-193. The discovery of a metal-free hydrogenase significantly alters our view of what components are necessary to make hydrogen. Even the metal-containing enzymes are likely to use aspects of the mechanism of this protein when is considered to be similar to the chemistry of alkanes in a superacidic solution.
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Arch Microbiol
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Hartmann, G.C.1
Klein, A.R.2
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Thauer, R.K.4
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0029731356
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Unleashing hydrogenase activity in pyruvate:ferredoxin oxidoreductase and acetyl-CoA synthase/CO dehydrogenase
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Menon S, Ragsdale SW: Unleashing hydrogenase activity in pyruvate:ferredoxin oxidoreductase and acetyl-CoA synthase/CO dehydrogenase. Biochemistry 1996, 35:15814-15821.
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Biochemistry
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0031046042
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A hydrogen-sensing system in transcriptional regulation of hydrogenase gene expression in Alcaligenes species
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••], describe a new class of gas-sensing proteins and how they can affect gene expression of enzymes that use or make that gas.
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Lenz, O.1
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2 activation of hupSLC transcription
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2 activation of hupSLC transcription. Mol Microbiol 1997, 26:927-937.
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Mol Microbiol
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24
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CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein
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Shelver D, Kerby RL, He YP, Roberts GP: CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. Proc Natl Acad Sci USA 1997, 94:11216-11220. This paper describes a new class of transcriptional activator that senses carbon monoxide (CO). It is shown to be similar to the cAMP receptor protein (CRP) but has a heme for sensing CO in the region that cAMP binds in CRP.
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Proc Natl Acad Sci USA
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Generation of active [NiFe] hygrogenase in vitro from a nickel-free precursor form
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Maier T, Bock A: Generation of active [NiFe] hygrogenase in vitro from a nickel-free precursor form. Biochemistry 1996, 35:235-241.
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Biochemistry
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Maier, T.1
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Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrphus requires the hoxW gene product
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Thiemermann, S.1
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Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
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Fox JD, Kerby RL, Roberts GP, Ludden PW: Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J Bacteriol 1 996, 178:1515-1524.
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Fox, J.D.1
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0028889166
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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
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Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fontecilla-Camps JC: Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 1995, 373:580-587.
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Structure of the [NiFe] hydrogenase active site: Evidence for biologically uncommon Fe ligands
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2 activation is a heterobimetallic complex and characterizes the diatomic molecules (CN and CO) bound to the Fe site.
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J am Chem Soc
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Volbeda, A.1
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0030799641
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Nature and electronic structure of the Ni-X dinuclear center of Desulfovibrio gigas hydrogenase. Implications for the enzymatic mechanism
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Dole F, Fournel A, Magro V, Hatchikian EC, Bertrand P, Guigliarelli B: Nature and electronic structure of the Ni-X dinuclear center of Desulfovibrio gigas hydrogenase. Implications for the enzymatic mechanism. Biochemistry 1997, 36:7847-7854.
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Fe-57 Q-band pulsed ENDOR of the heterodinuclear site of nickel hydrogenase: Comparison of NiA, NiB, and NiC states
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Huyett JE, Carepo M, Pamplona A, Franco R, Moura I, Moura JJG, Hoffman BM: Fe-57 Q-band pulsed ENDOR of the heterodinuclear site of nickel hydrogenase: comparison of NiA, NiB, and NiC states. J Am Chem Soc 1 997, 119:9291-9292.
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Similarities in the architecture of the active sites of Ni- Hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy
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Vanderspek TM, Arendsen AF, Happe RP, Yun SY, Bagley KA, Stufkens DJ, Hagen WR, Albracht SPJ: Similarities in the architecture of the active sites of Ni- hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy. Eur J Biochem 1996, 237:629-634.
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Eur J Biochem
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Vanderspek, T.M.1
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Infrared spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio gigas
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deLacey AL, Hatchikian EC, Volbeda A, Frey M, Fontecilla-Camps JC, Fernandez VM: Infrared spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio gigas. J Am Chem Soc 1997, 119:7181-7189. A very nice paper that shows that the shifts in the stretching frequency of the CN and CO ligands track the same series of states as the electron paramagnetic resonance (EPR) signal associated with the Ni site. Thus, IR can be used to probe all redox states of hydrogenase - EPR-active and EPR-silent. The paper showed that there are two EPR-silent states and that a protonation event converts one of these silent states into another state.
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J am Chem Soc
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Delacey, A.L.1
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Analysis of an organometallic iron site model for the heterodimetallic unit of [NiFe] hydrogenase
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Darensbourg DJ, Reibenspies JH, Lai CH, Lee WZ, Darensbourg MY: Analysis of an organometallic iron site model for the heterodimetallic unit of [NiFe] hydrogenase. J Am Chem Soc 1997, 119:7903-7904.
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Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
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Studies of light-induced nickel EPR signals in hydrogenase: Comparison of enzymes with and without selenium
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Medina M, Hatchikian EC, Cammack R: Studies of light-induced nickel EPR signals in hydrogenase: comparison of enzymes with and without selenium. Biochem Biophys Acta 1996, 1275:227-236.
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Biochem Biophys Acta
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Spin-spin interactions between the Ni site and the [4Fe-4S] centers as a probe of light-induced structural changes in active Desulfovibrio gigas hydrogenase
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Dole F, Medina M, More C, Cammack R, Bertrand P, Guigliarelli B: Spin-spin interactions between the Ni site and the [4Fe-4S] centers as a probe of light-induced structural changes in active Desulfovibrio gigas hydrogenase. Biochemistry 1996, 35:16399-16406.
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Reactions of H2 with the nickel site(s) of the [FeNi] and [FeNiSe] hydrogenase: What do the model complexes suggest?
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J Biol Inorg Chem
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Ragsdale SW, Kumar M: Ni containing carbon monoxide dehydrogenase/acetyl-CoA synthase. Chem Rev 1996, 96:2515-2539. This manuscript reviews the structure and function of carbon monoxide dehydrogenase (CODH) and CODH/acetyl-CoA synthase and relevant model chemistry.
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Ragsdale SW, Riordan CG: The role of nickel in acetyl-CoA synthesis by the bifunctional enzyme CO dehydrogenase/acetyl-CoA synthase: enzymology and model chemistry. J Bioinorg Chem 1996, 1:489-493.
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J Bioinorg Chem
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Carbon monoxide dehydrogenase from Clostridium thermoaceticum: Quaternary structure, stoichiometry of its SDS-induced dissociation, and characterization of the faster-migrating form
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Xia JQ, Sinclair JF, Baldwin TO, Lindahl PA: Carbon monoxide dehydrogenase from Clostridium thermoaceticum: quaternary structure, stoichiometry of its SDS-induced dissociation, and characterization of the faster-migrating form. Biochemistry 1996, 35:1965-1971.
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EXAFS, EPR, and electronic absorption spectroscopic study of the alpha metallosubunit of CO dehydrogenase from Clostridium thermoaceticum
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