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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Wever R, van GELDER B F, Dervartanian D V

Biochim Biophys Acta. 1975 May 15;387(2):189-93. doi: 10.1016/0005-2728(75)90102-4.

Upon addition of sulphide to oxidized cytochrome c oxidase, a low-spin heme sulphide compound is formed with an EPR signal at gx = 2.54, gy = 2.23 and gz = 1.87. Concomitantly with the formation of this signal the EPR-detectable low-spin heme signal at g = 3 and the copper signal near g = 2 decrease in intensity, pointing to a partial reduction of the enzyme by sulphide. 2. The addition of sulphide to cytochrome c oxidase, previously reduced in the presence of azide or cyanide, brings about a disappearance of the azido-cytochrome c oxidase signal at gx = 2.9, gy = 2.2, and gz = 1.67 and a decrease of the signal at g = 3.6 of cyano-cytochrome c oxidase. Concomitantly the sulphide-induced EPR signal is formed. 3. These observations demonstrate that azide, cyanide and sulphide are competitive for an oxidized binding site on cytochrome c oxidase. Moreover, it is shown that the affinity of cyanide and sulphide for this site is greater than that of azide.

向氧化型细胞色素c氧化酶中添加硫化物后，会形成一种低自旋血红素硫化物化合物，其电子顺磁共振（EPR）信号为gx = 2.54，gy = 2.23，gz = 1.87。伴随该信号的形成，g = 3处可通过EPR检测到的低自旋血红素信号以及g = 2附近的铜信号强度降低，这表明硫化物使该酶发生了部分还原。2. 向先前在叠氮化物或氰化物存在下已被还原的细胞色素c氧化酶中添加硫化物，会导致叠氮化物 - 细胞色素c氧化酶在gx = 2.9、gy = 2.2和gz = 1.67处的信号消失，以及氰化物 - 细胞色素c氧化酶在g = 3.6处的信号减弱。同时会形成硫化物诱导的EPR信号。3. 这些观察结果表明，叠氮化物、氰化物和硫化物对细胞色素c氧化酶上的氧化结合位点具有竞争性。此外，还表明氰化物和硫化物对该位点的亲和力大于叠氮化物。

Wever R, van GELDER B F, Dervartanian D V

Biochim Biophys Acta. 1975 May 15;387(2):189-93. doi: 10.1016/0005-2728(75)90102-4.

Upon addition of sulphide to oxidized cytochrome c oxidase, a low-spin heme sulphide compound is formed with an EPR signal at gx = 2.54, gy = 2.23 and gz = 1.87. Concomitantly with the formation of this signal the EPR-detectable low-spin heme signal at g = 3 and the copper signal near g = 2 decrease in intensity, pointing to a partial reduction of the enzyme by sulphide. 2. The addition of sulphide to cytochrome c oxidase, previously reduced in the presence of azide or cyanide, brings about a disappearance of the azido-cytochrome c oxidase signal at gx = 2.9, gy = 2.2, and gz = 1.67 and a decrease of the signal at g = 3.6 of cyano-cytochrome c oxidase. Concomitantly the sulphide-induced EPR signal is formed. 3. These observations demonstrate that azide, cyanide and sulphide are competitive for an oxidized binding site on cytochrome c oxidase. Moreover, it is shown that the affinity of cyanide and sulphide for this site is greater than that of azide.

向氧化型细胞色素c氧化酶中添加硫化物后，会形成一种低自旋血红素硫化物化合物，其电子顺磁共振（EPR）信号为gx = 2.54，gy = 2.23，gz = 1.87。伴随该信号的形成，g = 3处可通过EPR检测到的低自旋血红素信号以及g = 2附近的铜信号强度降低，这表明硫化物使该酶发生了部分还原。2. 向先前在叠氮化物或氰化物存在下已被还原的细胞色素c氧化酶中添加硫化物，会导致叠氮化物 - 细胞色素c氧化酶在gx = 2.9、gy = 2.2和gz = 1.67处的信号消失，以及氰化物 - 细胞色素c氧化酶在g = 3.6处的信号减弱。同时会形成硫化物诱导的EPR信号。3. 这些观察结果表明，叠氮化物、氰化物和硫化物对细胞色素c氧化酶上的氧化结合位点具有竞争性。此外，还表明氰化物和硫化物对该位点的亲和力大于叠氮化物。