Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules.
about
Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site.The low-affinity complex of cytochrome c and its peroxidaseControl of cyclic photoinitiated electron transfer between cytochrome c peroxidase (W191F) and cytochrome c by formation of dynamic binary and ternary complexes.Thirty years of heme peroxidase structural biology.
P2860
Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules.
description
2006 nî lūn-bûn
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2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
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2006年论文
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2006年论文
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name
Characterization of four coval ...... bound cytochrome c molecules.
@en
type
label
Characterization of four coval ...... bound cytochrome c molecules.
@en
prefLabel
Characterization of four coval ...... bound cytochrome c molecules.
@en
P2093
P2860
P356
P1433
P1476
Characterization of four coval ...... bound cytochrome c molecules.
@en
P2093
James E Erman
Lidia B Vitello
Siddhartha Nakani
P2860
P304
14371-14378
P356
10.1021/BI061662P
P407
P577
2006-12-01T00:00:00Z