Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha

Biochemistry

Volumn 36, Issue 51, 1997, Pages 16267-16276

  Cheesman, Myles R ^a   Ferguson, Stuart J ^a   Moir, James W B ^b   Richardson, David J ^c   Zumft, Walter G ^d   Thomson, Andrew J ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF SHEFFIELD   (United Kingdom)

^d UNIVERSITY OF KARLSRUHE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; CYTOCHROME D; HEME DERIVATIVE; NITRITE REDUCTASE;

ARTICLE; DENITRIFICATION; ENZYME ISOLATION; LIGAND BINDING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PSEUDOMONAS STUTZERI;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; CYTOCHROMES; ELECTRON SPIN RESONANCE SPECTROSCOPY; GRAM-NEGATIVE CHEMOLITHOTROPHIC BACTERIA; HEME; IRON; MOLECULAR SEQUENCE DATA; NITRITE REDUCTASES; PSEUDOMONAS; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY;

BACTERIA (MICROORGANISMS); PARACOCCUS PANTOTROPHUS; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS STUTZERI; THIOCYSTIS;

EID: 0031423110     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971677a     Document Type: Article

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