Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244

被引:262
作者
Proshlyakov, DA
Pressler, MA
DeMaso, C
Leykam, JF
DeWitt, DL
Babcock, GT [1 ]
机构
[1] Michigan State Univ, Dept Chem, E Lansing, MI 48824 USA
[2] Michigan State Univ, Dept Biochem, E Lansing, MI 48824 USA
关键词
D O I
10.1126/science.290.5496.1588
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Cytochrome oxidase activates and reduces O-2 to water to sustain respiration and uses the energy released to drive proton translocation and adenosine 5'-triphosphate synthesis. A key intermediate in this process, P, lies at the junction of the O-2-reducing and proton-pumping functions. We used radioactive iodide labeling followed by peptide mapping to gain insight into the structure of P. We show that the cross-linked histidine 240-tyrosine 244 (His(240)-Tyr(244) species is redox active in P formation, which establishes its structure as Fe-IV=O/(CuB2+H240)-Y-244. Thus, energy transfer from O-2 to the protein moiety is used as a strategy to avoid toxic intermediates and to control energy utilization in subsequent proton-pumping events.
引用
收藏
页码:1588 / 1591
页数:4
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