Results 271 to 280 of about 468,888 (313)
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C-type cytochromes of Desulfovibrio vulgaris the primary structure of cytochrome c553
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972Abstract The amino acid sequence of cytochrome c553 from Desulfovibrio vulgaris (NCIB 8303) is presented. The protein molecule consists of a single polypeptide chain of 82 residues. This sequence is deduced from data obtained by enzymatic digestion of the apoprotein or by chemical cleavage with cyanogen bromide.
Mireille Bruschi +2 more
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Resonance Raman spectroscopy of c-type cytochromes
Biochimie, 1994This paper provides an overview of the usefulness of the resonance Raman (RR) spectroscopy in the determination of the structural and electronic properties of heme(s) included in c-type cytochromes. It reviews the mode assignments presently available for heme c and includes recent RR data on the most important subclasses of c-type cytochromes.
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Bacterial c-type cytochromes and pathogenicity
European Journal of BioMedical Research, 2015During the course of infection, bacterial pathogens must adjust their metabolism for growth in the host and to counteract host response systems that would otherwise eliminate the pathogen. A group of proteins that can participate in such metabolic shifts are the c -type cytochromes, a widely distributed class of extracellular hemoprotiens involved in ...
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Electrochemical studies on c-type cytochromes at microelectrodes
Journal of Electroanalytical Chemistry, 1999The aim of this work is to use microelectrodes as a current approach for the study of unmediated electrochemistry of redox proteins. An electrochemical study of monohemic cytochromes c552 from Pseudomonas nautica 617, cytochrome c553 from Desulfovibrio vulgaris and horse heart cytochrome c is presented at inlaid disk microelectrodes of platinum, gold ...
M.M. Correia dos Santos +5 more
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Electron transport by C-type cytochromes
Biophysics of Structure and Mechanism, 1975The kinetics of reduction of horse heartcytochrome c have been investigated using the reductants sodium dithionite and potassium ferrocyanide. Sodium dithionite reduction at pH 7.0 yields rate constants of 2.8 X 10(8)M(-1)sec-1 for SO2 AND 6 X 10(5) M-1 sec-1 for S2O4 at infinite dilution.
W G, Miller, M A, Cusanovich
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The role of C-type cytochrome in the Hill reaction with Euglena chloroplasts
Archives of Biochemistry and Biophysics, 1967Abstract Euglena chloroplasts catalyze the Hill reaction with ferricyanide or dichlorophenol indophenol (DPIP) but not with nicotinamide adenine dinucleotide phosphate (NADP), methyl viologen or horse-heart cytochrome c . The latter compounds can serve as Hill oxidants with Euglena chloroplasts provided Euglena cytochrome-552 is included in ...
S, Katoh, A, San Pietro
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Why do c-type cytochromes exist? — Reprise
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991An earlier paper (Wood, P.M. (1983) FEBS Lett. 164, 223-226) proposed that the covalent links that characterize c-type haem originated in order to prevent the haem being lost into the external medium. This is discussed in relation to Gram-negative and Gram-positive bacteria, cyanobacterial thylakoids and eukaryotes.
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Resonance Raman spectra of the b- And c-type cytochromes of succinate-cytochrome c reductase
Archives of Biochemistry and Biophysics, 1974Abstract 1. Resonance Raman spectra excited by laser photons in resonance with the α and β electronic transitions of the reduced forms of cytochrome b 5 and c were recorded and used as model systems to distinguish the “ b ”- and “ c ”-type Cytochromes of succinate-cytochrome c reductase. 2.
F, Adar, M, Erecińska
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Resolution, Characterisation and Classification of c-Type Cytochromes
1987Functional studies of cytochromes fall into one of two groups. In the first, the intact respiratory system is examined using methods which allow the resolution of individual components. In the second, components are isolated and characterised and their role studied in reconstituted partial systems. Relatively few studies incorporate both approaches and
Graham W. Pettigrew, Geoffrey R. Moore
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Cytochrome c′-type cytochrome-c peroxidase derived from Nitrosomonas europaea
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986Abstract From Nitrosomonas europaea , a cytochrome c ′-type haem protein has been purified which has cytochrome- c peroxidase (ferrocytochrome- c :hydrogen-peroxide oxidoreductase, EC 1.11.1.5) activity. The protein has haem c and shows the high-spin-type absorption spectra: it shows absorption peaks at 400, 500 and 640 nm in the oxidized form ...
Takeshi Yamazaki +2 more
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