Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state

European Journal of Biochemistry

Volumn 267, Issue 13, 2000, Pages 4205-4212

  Pristovšek, Primož ^c   Lücke, Christian ^c   Reincke, Britta ^c   Ludwig, Bernd ^c   Rüterjans, Heinz ^a,b  

^a Inst F Biophysikalische Chemie   (Germany)

^b NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^c NONE

Author keywords

Cytochrome c552; Heme; Isotope enrichment 15N ; NMR spectroscopy; Redox states

Indexed keywords

CYTOCHROME C OXIDASE;

ARTICLE; ENZYME ANALYSIS; ENZYME STRUCTURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; OXIDATION REDUCTION STATE; PARACOCCUS DENITRIFICANS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CRYSTALLIZATION; CYTOCHROME C GROUP; HYDROGEN BONDING; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PARACOCCUS DENITRIFICANS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

BACTERIA (MICROORGANISMS); PARACOCCUS DENITRIFICANS;

EID: 0000887409     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01456.x     Document Type: Article

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