Increasing the redox potential of isoform 1 of yeast cytochrome c through the modification of select haem interactions.
about
Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucosideConstraints on the Radical Cation Center of Cytochrome c Peroxidase for Electron Transfer from Cytochrome cRemote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersThe role of key residues in structure, function, and stability of cytochrome-c.Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.Topological and electron-transfer properties of yeast cytochrome c adsorbed on bare gold electrodes.The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c
P2860
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P2860
Increasing the redox potential of isoform 1 of yeast cytochrome c through the modification of select haem interactions.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
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2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
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2002年學術文章
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name
Increasing the redox potential ...... n of select haem interactions.
@en
Increasing the redox potential ...... n of select haem interactions.
@nl
type
label
Increasing the redox potential ...... n of select haem interactions.
@en
Increasing the redox potential ...... n of select haem interactions.
@nl
prefLabel
Increasing the redox potential ...... n of select haem interactions.
@en
Increasing the redox potential ...... n of select haem interactions.
@nl
P2860
P1433
P1476
Increasing the redox potential ...... n of select haem interactions.
@en
P2093
C Marc Lett
J Guy Guillemette
P2860
P304
P356
10.1042/0264-6021:3620281
P407
P577
2002-03-01T00:00:00Z