Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy.
Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy.
复制标题
通过共振拉曼光谱法对细胞色素 c 氧化酶的双氧中间体进行室温表征。
DOI：
10.1021/bi00495a018
复制
发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Ondrias,MR
中科院分区：
文献类型：
--
作者：
Larsen,RW;Li,W;Copeland,RA;Witt,SN;Lou,BS;Chan,SI;Ondrias,MR
摘要：利用共振曼光谱研究了室温下细胞色素c氧化酶催化中间体的血红素结构。得到了化合物C（二电子还原的二氧中间体）、铁基（三电子还原的二氧中间体）和完全氧化酶的高频共振拉曼光谱。化合物C是由CO混合价酶在02存在下光解生成的。铁基中间体是通过过量的H202使完全还原酶再氧化而形成的。用02对完全还原的酶进行再氧化，制备了两种形式的氧化酶。我们的数据表明，在化合物C中，cyta3为中自旋或低自旋，不耐光，其氧化态标记带p4出现的频率高于酶的静止形式。铁基中间体也显示出低自旋cyt s3，这是不耐光的，并且氧化态标记带v4的频率更高。细胞色素c氧化酶的再氧化形式在420 nm处具有Soret吸收最大值，其氧化态标记带（p4）的位置与静止形式相似，而自旋态区域与化合物c相似。该物种随后衰变为酶的第二氧化形式，其显示出与原始静止酶相同的高频共振拉曼光谱。细胞色素c氧化酶是一种多亚基膜结合蛋白，催化线粒体中二氧的四电子还原。酶的氧还原活性与呼吸过程中质子在线粒体内膜上的移位有关。该酶利用四个氧化还原活性金属中心来执行其催化功能。这些中心包括两个血红素A发色团和两个Cu离子。二氧还原位点由双核血红素a /Cu簇（称为细胞色素a3， CuB）组成。剩下的两个金属中心（指定为cyt a和CuA）介导电子从铁细胞色素c到细胞色素的转移
Revised Manuscript Received July 30, 1990 abstract: ResonanceRaman spectroscopy was employed to investigate the heme structures of catalytic intermediates of cytochrome c oxidase at room temperature. The high-frequency resonance Raman spectra were obtained for compound C (the two-electron-reduced dioxygen intermediate), ferryl (the three-electron-reduced dioxygen intermediate), and the fully oxidized enzyme. Compound C was formed by photolyzing CO mixed-valence enzyme in the presence of 02. The ferryl intermediate was formed by reoxidation of the fully reduced enzyme by an excess of H202. Two forms of the oxidized enzyme were prepared by reoxidizing the fully reduced enzyme with 02. Our data indicate that, in compound C, cyt a3 is either intermediate or low spin and is nonphotolabile and its oxidation state marker band, p4, appears at a higher frequency than that of the restingform of the enzyme. The ferryl intermediate also displays a low-spin cyt s3, which is nonphotolabile, and an even higher frequency for the oxidation state marker band, v4. The reoxidized form of cytochrome c oxidase with a Soret absorption maximum at 420 nm has an oxidation state marker band (p4) in a position similar to that of the resting form, while the spin-state region resembles that of compound C. This species subsequently decays to a second oxidized form of the enzyme, which displays a high-frequency resonance Raman spectrum identicalwith that of the original restingenzyme.(Cytochrome c oxidase is a multisubunit, membrane-bound protein that catalyzes the four-electron reduction of dioxygen in mitochondria. The oxygen reduction activity of the enzyme is coupled to proton translocation across the inner mitochon-drial membrane during respiration. The enzyme utilizes four redox-active metal centers to perform its catalytic function. These centers include two heme A chromophores and two Cu ions. The dioxygen reduction site consists of a binuclear heme A/Cu cluster (designated cytochrome a3, CuB). The two remaining metal centers (designated cyt a and CuA) mediate the electron transfer from ferrocytochrome c to cytochrome
登录
查看更多内容
可通过 EPR 光谱检测细胞色素 C 氧化酶的成分。
DOI：
10.1016/0005-2728(74)90178-9
发表时间：
1974
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
C. Hartzell;Helmut Beinert
通讯作者：
Helmut Beinert
低温下傅里叶变换红外光谱研究牛心线粒体细胞色素c氧化酶中CO与a3Fe和CuB的动态相互作用。
DOI：
10.1016/s0021-9258(19)68085-3
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
F. G. Fiamingo;R. Altschuld;P. P. Moh;J. O. Alben
通讯作者：
J. O. Alben
细胞色素c氧化酶在低温下催化双氧还原的机制。
DOI：
--
发表时间：
1985
期刊：
影响因子：
--
作者：
D. Blair;S. N. Witt;S. Chan
通讯作者：
S. Chan
细胞色素氧化酶还原氧的早期中间体中 .nu.(Fe-O) 的时间分辨拉曼检测
DOI：
--
发表时间：
1989
期刊：
影响因子：
--
作者：
C. Varotsis;W. Woodruff;G. Babcock
通讯作者：
G. Babcock
DOI：
10.1016/s0021-9258(18)67355-7
发表时间：
1986-08
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
S. Hashimoto;J. Teraoka;T. Inubushi;T. Yonetani;T. Kitagawa
通讯作者：
S. Hashimoto;J. Teraoka;T. Inubushi;T. Yonetani;T. Kitagawa