Q-band ENDOR spectra of the Rieske protein from Rhodobacter capsulatus ubiquinol-cyctochrome c oxidoreductase show two histidines coordinated to the (2Fe-2S) cluster

Journal Article · Tue Dec 10 04:00:00 EST 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00113a013· OSTI ID:5617519

Gurbiel, R J ^[1]; Ohnishi, Tomoko; Robertson, D E; Daldal, F ^[2]; Hoffman, B M ^[3]

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1. Northwestern Univ., Evanston, IL (United States) Jagiellonian Univ., Krakow (Poland)
2. Univ. of Pennsylvania, Philadelphia (United States)
3. Northwestern Univ., Evanston, IL (United States)

Electron nuclear double resonance (ENDOR) experiments were performed on {sup 14}N (natural abundance) and {sup 15}N-enriched iron-sulfur Rieske protein in the ubiquinol-cytochrome c{sub 2} oxidoreductase from Rhodobactor capsulatus. The experiments proved that two distinct nitrogenous ligands, histidines, are undoubtedly ligated to the Rieske (2Fe-2S) center. The calculations of hyperfine tensors give values similar but not identical to those of the Rieske-type cluster in phthalate dioxygenase of Pseudomonas cepacia and suggest a slightly different geometry of the iron-sulfur cluster in the two proteins.

• OSTI ID: 5617519
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:49; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
AZOLES
BACTERIA
CARBOXYLIC ACIDS
CYTOCHROMES
ELECTRON SPECTRA
ENDOR
ENZYMES
GEOMETRY
HEME
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
HYPERFINE STRUCTURE
IMIDAZOLES
ISOTOPES
LIGANDS
LIGHT NUCLEI
MAGNETIC RESONANCE
MATHEMATICS
MICROORGANISMS
NITROGEN 14
NITROGEN 15
NITROGEN ISOTOPES
NUCLEI
ODD-EVEN NUCLEI
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDOREDUCTASES
PIGMENTS
PORPHYRINS
PROTEINS
PSEUDOMONAS
RESONANCE
SPECTRA
STABLE ISOTOPES