Characterization and redox properties of high molecular mass cytochrome c3 (Hmc) isolated from Desulfovibrio vulgaris Miyazaki
- 31 December 1993
- Vol. 75 (11) , 977-983
- https://doi.org/10.1016/0300-9084(93)90148-l
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 18 references indexed in Scilit:
- Amino acid sequence and function of rebredoxin from Desulfovibrio vulgaris MiyazakiBiochimie, 1989
- EPR study of the redox interactions in cytochrome c3 from Desulfovibrio vulgaris MiyazakiEuropean Journal of Biochemistry, 1989
- Comparative studies of polyhemic cytochromes c isolated from Desulfovibriovulgaris (Hildenborough) and Desulfovibrio, desulfuricans (Norway)Biochemical and Biophysical Research Communications, 1989
- Characterization and complete amino acid sequence of ferrodoxin II from Desulfovibrio vulgaris MiyazakiBiochimie, 1988
- Isolation and crystallization of high molecular weight cytochrome from Desulfovibrio valgaris HildenboroughBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Refined structure of cytochrome c3 at 1.8 Å resolutionJournal of Molecular Biology, 1984
- Cytochrome c3, tetrahemoprotein electron carrier found in sulfate-reducing bacteriaAccounts of Chemical Research, 1983
- Purification and properties of cytochrome c-553, an electron acceptor for formate dehydrogenase of Desulfovibrio vulgaris, MiyazakiBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964