An EPR, ESEEM, structural NMR, and DFT study of a synthetic model for the covalently ring-linked tyrosine-histidine structure in the heme-copper oxidases.
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Identification of a histidine-tyrosine cross-link in the active site of the cbb3-type cytochrome c oxidase from Rhodobacter sphaeroidesAminoxyl Radicals of B/P Frustrated Lewis Pairs: Refinement of the Spin-Hamiltonian Parameters by Field- and Temperature-Dependent Pulsed EPR Spectroscopy.Two tyrosyl radicals stabilize high oxidation states in cytochrome C oxidase for efficient energy conservation and proton translocation.A spectroscopic investigation of a tridentate Cu-complex mimicking the tyrosine-histidine cross-link of cytochrome C oxidase.
P2860
An EPR, ESEEM, structural NMR, and DFT study of a synthetic model for the covalently ring-linked tyrosine-histidine structure in the heme-copper oxidases.
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2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
An EPR, ESEEM, structural NMR, ...... e in the heme-copper oxidases.
@en
An EPR, ESEEM, structural NMR, ...... e in the heme-copper oxidases.
@nl
type
label
An EPR, ESEEM, structural NMR, ...... e in the heme-copper oxidases.
@en
An EPR, ESEEM, structural NMR, ...... e in the heme-copper oxidases.
@nl
prefLabel
An EPR, ESEEM, structural NMR, ...... e in the heme-copper oxidases.
@en
An EPR, ESEEM, structural NMR, ...... e in the heme-copper oxidases.
@nl
P2093
P356
P1476
An EPR, ESEEM, structural NMR, ...... re in the heme-copper oxidases
@en
P2093
Clifford J Unkefer
Constantino Aznar
Louis A Silks
Marcin Brynda
R David Britt
Sun Hee Kim
William H Woodruff
P304
P356
10.1021/JA0303743
P407
P577
2004-03-01T00:00:00Z