Long-distance cofactor interactions in terminal oxidases studied by second-derivative absorption spectroscopy.
Long-distance cofactor interactions in terminal oxidases studied by second-derivative absorption spectroscopy.
复制标题
通过二阶导数吸收光谱研究末端氧化酶中的长距离辅因子相互作用。
DOI：
10.1007/bf00762851
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发表时间：
1993
影响因子：
3
通讯作者：
Copeland,RA
中科院分区：
文献类型：
--
作者：
Copeland,RA
The electronic transitions of the two heme groups of cytochromecoxidase have been resolved by application of second-derivative and cryogenic absorption spectroscopy. Both methods reveal a splitting of the ferrocytochromeaSoret transition into two features at 443 and 450 nm. The relative intensity of the 450 nm feature appears to depend on the ligation state of cytochromea3, the solution pH, and complex formation with cytochromec. The structural origin and mechanistic significance of this second Soret transition of cytochromeaare discussed in terms of the electron transfer and proton translocation activities of the enzyme.
