EPR studies of wild-type and several mutants of cytochrome c oxidase from Rhodobacter sphaeroides: Glu286 is not a bridging ligand in the cytochrome a3-CuB center

FEBS Letters

Volumn 374, Issue 3, 1995, Pages 371-374

  Mitchell, David M ^a,b   Aasa, Roland ^b   Ädelroth, Pia ^b   Brzezinski, Peter ^b   Gennis, Robert B ^a   Malmström, Bo G ^b  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

Bimetallic cytochrome a3 CuB; Cytochrome a; Cytochrome oxidase; EPR spectroscopy; Rhodobacter sphaeroides

Indexed keywords

CYTOCHROME C OXIDASE;

ARTICLE; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; MUTANT; PRIORITY JOURNAL; RHODOBACTER SPHAEROIDES;

BASE SEQUENCE; COPPER; CYTOCHROME A; CYTOCHROME-C OXIDASE; ELECTRON SPIN RESONANCE SPECTROSCOPY; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; RHODOBACTER SPHAEROIDES;

BACTERIA (MICROORGANISMS); MAMMALIA; RHODOBACTER SPHAEROIDES; RHODOPSEUDOMONAS;

EID: 0028784210     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(95)01149-9     Document Type: Article

References (17)

1. Interconversion of Fast and Slow Forms of Cytochrome bo from Escherichia coli