Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Moessbauer spectra

Journal Article · Fri Jun 01 04:00:00 EDT 1984 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.81.12.3728· OSTI ID:5975779

Huynh, B H; Czechowski, M H; Krueger, H J; DerVartanian, D V; Peck, Jr, H D; LeGall, J

A purification procedure for the periplasmic hydrogenase from Desulfovibrio vulgaris is reported. The purified hydrogenase has a specific activity of 4800 units per mg of protein. Plasma emission studies reveal that this highly active hydrogenase is free of nickel and contains 11 (+/-1) nonheme iron atoms per molecule. A combined EPR and Moessbauer study indicates that the majority of the iron atoms are bound in the form of iron-sulfur clusters. Two ferredoxin-type (4Fe-4S) clusters have been identified that exhibit normal EPR and Moessbauer parameters; however, no trace of 3Fe cluster is detected by the Moessbauer measurement. In the presence of oxidants, cytochrome c/sub 3/, and CO, anomalous EPR and Moessbauer spectra indicative of atypical nonheme iron centers are observed. 24 references, 5 figures, 1 table.

• Research Organization: Univ. of Georgia, Athens
• DOE Contract Number: AT03-79ER10491
• OSTI ID: 5975779
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 81:12; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
CARBOXYLIC ACIDS
DESULFOVIBRIO
ELECTRON SPIN RESONANCE
ELEMENTS
ENZYMES
HEME
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYDROGENASES
MAGNETIC RESONANCE
METALS
MICROORGANISMS
NICKEL
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDOREDUCTASES
PIGMENTS
PORPHYRINS
PROTEINS
PURIFICATION
RESONANCE
STRUCTURAL CHEMICAL ANALYSIS
SULFATE-REDUCING BACTERIA
TRANSITION ELEMENTS