The heme-containing N-fragment (residues 1-56) of cytochrome c is a bis-histidine functional system

Archives of Biochemistry and Biophysics

Volumn 379, Issue 2, 2000, Pages 331-336

  Santucci, Roberto ^a   Fiorucci, Laura ^a   Sinibaldi, Federica ^a   Polizio, Francesca ^a   Desideri, Alessandro ^a   Ascoli, Franca ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

Circular dichroism; Cytochrome c; Electrochemistry; N fragment

Indexed keywords

CYTOCHROME C OXIDASE; HEME; HISTIDINE;

ARTICLE; CIRCULAR DICHROISM; ELECTROCHEMISTRY; ENZYME ANALYSIS; ENZYME STRUCTURE; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PKA; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT;

EID: 0034661403     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.2000.1885     Document Type: Article

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