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Kinetics and interaction studies between cytochrome c 3 and Fe‐only hydrogenase from Desulfovibrio vulgaris hildenborough
Author(s) -
Brugna Marianne,
GiudiciOrticoni M.T.,
Spinelli Silvia,
Brown Kieron,
Tegoni Mariella,
Bruschi Mireille
Publication year - 1998
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19981201)33:4<590::aid-prot11>3.0.co;2-i
Subject(s) - hydrogenase , desulfovibrio vulgaris , chemistry , electron transfer , cytochrome , desulfovibrio , electron transport chain , cooperativity , crystallography , cytochrome c , kinetics , biochemistry , bacteria , enzyme , biology , organic chemistry , sulfate , mitochondrion , genetics , physics , quantum mechanics
Hydrogenases from Desulfovibrio are found to catalyze hydrogen uptake with low potential multiheme cytochromes, such as cytochrome c 3 , acting as acceptors. The production of Fe‐only hydrogenase from Desulfovibrio vulgaris Hildenborough was improved with respect to the growth phase and media to determine the best large‐scale bacteria growth conditions. The interaction and electron transfer from Fe‐only hydrogenase to multiheme cytochrome has been studied in detail by both BIAcore and steady‐state measurements. The electron transfer between [Fe] hydrogenase and cytochrome c 3 appears to be a cooperative phenomenon (h = 1.37). This behavior could be related to the conductivity properties of multihemic cytochromes. An apparent dissociation constant was determined (2 × 10 ‐7 M). The importance of the cooperativity for contrasting models proposed to describe the functional role of the hydrogenase/cytochrome c 3 complex is discussed. Presently, the only determined structure is from [NiFe] hydrogenase and there are no obvious similarities between [NiFe] and [Fe] hydrogenase. Furthermore, no crystallographic data are available concerning [Fe] hydrogenase. The first results on crystallization and X‐ray crystallography are reported. Proteins 33:590–600, 1998. © 1998 Wiley‐Liss, Inc.