Title : The binding of porphyrin cytochrome c to yeast cytochrome c peroxidase. A fluorescence study of the number of sites and their sensitivity to salt.

Pub. Date : 1986 Mar 17

PMID : 3007133






7 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Porphyrin c, the iron-free derivative of cytochrome c, is a reasonably good model for cytochrome c binding to cytochrome c peroxidase (CcP). porphyrin c cytochrome-c peroxidase Saccharomyces cerevisiae S288C
2 Porphyrin c, the iron-free derivative of cytochrome c, is a reasonably good model for cytochrome c binding to cytochrome c peroxidase (CcP). porphyrin c cytochrome-c peroxidase Saccharomyces cerevisiae S288C
3 Porphyrin c, the iron-free derivative of cytochrome c, is a reasonably good model for cytochrome c binding to cytochrome c peroxidase (CcP). Iron cytochrome-c peroxidase Saccharomyces cerevisiae S288C
4 Porphyrin c, the iron-free derivative of cytochrome c, is a reasonably good model for cytochrome c binding to cytochrome c peroxidase (CcP). Iron cytochrome-c peroxidase Saccharomyces cerevisiae S288C
5 The binding of porphyrin c to the cyano form and the resting forms of CcP cannot be distinguished by our methods. porphyrin c cytochrome-c peroxidase Saccharomyces cerevisiae S288C
6 The calculated distances between porphyrin c and the hemes of CcP(FeIII) and ES are approximately 2.5 nm. porphyrin c cytochrome-c peroxidase Saccharomyces cerevisiae S288C
7 The calculated distances between porphyrin c and the hemes of CcP(FeIII) and ES are approximately 2.5 nm. Heme cytochrome-c peroxidase Saccharomyces cerevisiae S288C