Characterization of the low-temperature intermediates of the reaction of fully reduced soluble cytochrome oxidase with oxygen by electron-paramagnetic-resonance and optical spectroscopy.
about
A novel mitochondrial signaling pathway activated by visible-to-near infrared radiation.Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a.Spectroscopic characterization of compound C and related derivatives of cytochrome oxidaseEnergy-dependent reversal of the cytochrome oxidase reaction.Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase.The oxygen reaction of the cytochrome d-terminated respiratory chain of Escherichia coli at sub-zero temperatures. Kinetic resolution by EPR spectroscopy of two high-spin cytochromes.Spectroscopic elucidation of a new heme/copper dioxygen structure type: implications for O···O bond rupture in cytochrome c oxidaseOxygen activation by cytochrome oxidase: a new spectral intermediate observed by flow-flash.New transients in the electron-transfer dynamics of photolyzed mixed-valence CO-cytochrome c oxidase.Cytochrome c oxidase: two models.The structure of the paramagnetic oxygen intermediate in the cytochrome c oxidase reaction.H2O2-induced conversion of cytochrome c oxidase peroxy complex to oxoferryl state.An investigation by e.p.r. and optical spectroscopy of cytochrome oxidase during turnover.The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.Characterization of the intermediates in the reaction of mixed-valence state soluble cytochrome oxidase with oxygen at low temperatures by optical and electron-paramagnetic-resonance spectroscopy.Characterization of the intermediates in the reaction of membrane-bound mixed-valence-state cytochrome oxidase with oxygen at low temperatures by optical spectroscopy in the visible region.How does cytochrome oxidase pump protons? A "cooperative proton pump" model.Electron transfer and conformation states in bovine cytochrome c oxidase.
P2860
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P2860
Characterization of the low-temperature intermediates of the reaction of fully reduced soluble cytochrome oxidase with oxygen by electron-paramagnetic-resonance and optical spectroscopy.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
1980年论文
@zh
1980年论文
@zh-cn
name
Characterization of the low-te ...... ance and optical spectroscopy.
@en
Characterization of the low-te ...... ance and optical spectroscopy.
@nl
type
label
Characterization of the low-te ...... ance and optical spectroscopy.
@en
Characterization of the low-te ...... ance and optical spectroscopy.
@nl
prefLabel
Characterization of the low-te ...... ance and optical spectroscopy.
@en
Characterization of the low-te ...... ance and optical spectroscopy.
@nl
P2093
P2860
P356
P1433
P1476
Characterization of the low-te ...... nance and optical spectroscopy
@en
P2093
B G Malmström
B Karlsson
L E Andréasson
P2860
P304
P356
10.1042/BJ1850139
P407
P577
1980-01-01T00:00:00Z