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Biochimica et Biophysica Acta - Bioenergetics

Volumn 1413, Issue 1, 1999, Pages 1-13

The caa3 terminal oxidase of the thermohalophilic bacterium Rhodothermus marinus: A HiPIP:oxygen oxidoreductase lacking the key glutamate of the D-channel

(9) Pereira, Manuela M a Santana, Margarida a Soares, Cláudio M a Mendes, Joaquim a Carita, Joáo N a Fernandes, Andreia S a Saraste, Matti b Carrondo, Maria A a Teixeira, Miguel a

a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA (Portugal)

b EUROPEAN MOLECULAR BIOLOGY LABORATORY (Germany)

Author keywords

High potential iron sulfur protein (HiPIP); Proton pathway; Rhodothermus marinus; Terminal oxidase; Thermophile

Indexed keywords

CYTOCHROME C; GLUTAMIC ACID; HEME; ION CHANNEL; IRON SULFUR PROTEIN; OXIDOREDUCTASE; PHENOL; TYROSINE; BACTERIAL PROTEIN; CYTOCHROME C OXIDASE; HIGH POTENTIAL IRON SULFUR PROTEIN; HIGH POTENTIAL IRON-SULFUR PROTEIN; N DEMETHYLASE; TETRAMETHYLPHENYLENEDIAMINE OXIDASE;

AMINO ACID SEQUENCE; BINDING SITE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME ISOLATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; HALOPHILIC BACTERIUM; METAL BINDING; MODEL; NONHUMAN; OXIDATION REDUCTION POTENTIAL; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTON TRANSPORT; REVIEW; RHODOTHERMUS MARINUS; SEQUENCE HOMOLOGY; THERMOPHILIC BACTERIUM; ARTICLE; CHEMISTRY; ELECTRON TRANSPORT; ENZYMOLOGY; GRAM NEGATIVE AEROBIC RODS AND COCCI; METABOLISM; MOLECULAR GENETICS; PHOTOSYNTHESIS; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY;

BACTERIA (MICROORGANISMS); EQUUS CABALLUS; RHODOTHERMUS MARINUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CYTOCHROME C GROUP; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; GLUTAMIC ACID; GRAM-NEGATIVE AEROBIC BACTERIA; IRON-SULFUR PROTEINS; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES, N-DEMETHYLATING; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY;

EID: 0032778747 PISSN: 00052728 EISSN: None Source Type: Journal
DOI: 10.1016/S0005-2728(99)00073-0 Document Type: Article

Times cited : (52)

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