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Titolo:
EPR study of soluble hydrogenase from photosynthetic bacteria Chromatium vinosum
Autore:
Long, MN; Su, WJ; Albracht, SPJ; Zhang, FZ; Xu, LS;
Indirizzi:
Xiamen Univ, Sch Life Sci, Key Lab, Minist Educ Cell Biol & Tumor Engineer, Xiamen 361005, Peoples R China Xiamen Univ Xiamen Peoples R China 361005 Xiamen 361005, Peoples R China Univ Amsterdam, EC Slater Inst, Amsterdam, Netherlands Univ Amsterdam Amsterdam Netherlands later Inst, Amsterdam, Netherlands
Titolo Testata:
CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE
fascicolo: 7, volume: 22, anno: 2001,
pagine: 1137 - 1140
SICI:
0251-0790(200107)22:7<1137:ESOSHF>2.0.ZU;2-H
Fonte:
ISI
Lingua:
CHI
Soggetto:
DESULFOVIBRIO-GIGAS; PROSTHETIC GROUPS; NIFE HYDROGENASE; ACTIVE-SITE; CHEMISTRY; READY;
Keywords:
Chromatium vinosum; soluble hydrogenase; EPR spectra;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Long, MN Xiamen Univ, Sch Life Sci, Key Lab, Minist Educ Cell Biol & TumorEngineer, Xiamen 361005, Peoples R China Xiamen Univ Xiamen Peoples R China 361005 1005, Peoples R China
Citazione:
M.N. Long et al., "EPR study of soluble hydrogenase from photosynthetic bacteria Chromatium vinosum", CHEM J CH U, 22(7), 2001, pp. 1137-1140

Abstract

A soluble hydrogenase(SH) was purified from Chromatium vinosum by five step chromatography(DE-23, TSK-DEAE(I), Ultragel AcA-44, TSK-DEAE(I), SuperdexTM75) with a specific activity of 8.4 mu mol H-Z/(min.mg prot). The oxidized SH yield two Ni( I) EPR(electron paramagnetic resonance) signals (g(x,y,z)=2.37, 2.16, 2.016 and g(x,y,z)=2.30, 2.23, 2.016) at 45 K which occurredin the other NiFe-hydrogenases. However, no [3Fe-4S] cluster EPR signal was obtained at 10 K. When the SH was reduced by H-2(over night at 8 degreesC), the Ni(I) EPR signals disappeared, and an EPR signal from a reduced[4Fe-4S] cluster appeared (g(x,y,z)=1.88, 1.90, 2.045). The results show that the soluble hydrogenase from C. vinosum is a new NiFe-hydrogenase which catalyzes H-2-production.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 10:00:51