Cytochrome c (cyt c) is one of the most studied conjugated proteins due to its electron-transfer properties and ability to regulate the processes involved in homeostasis or apoptosis. Here we report an electrochemical strategy for investigating the electroactivity of cyt c and its analogs with a disrupted heme moiety, i.e. apocytochrome c (acyt c) and porphyrin cytochrome c (pcyt c). The electrochemical data are supplemented with low-temperature and spin-probe electron paramagnetic resonance (EPR) spectroscopy. The main contribution of this report is a complex evaluation of cyt c reduction and oxidation at the level of surface-localized amino acid residues and the heme moiety in a single electrochemical scan. The electrochemical pattern of cyt c is substantially different to both analogs acyt c and pcyt c, which could be applicable in further studies on the redox properties and structural stability of cytochromes and other hemeproteins.

细胞色素c（cyt c）由于其电子转移特性和调节稳态或凋亡过程的能力而成为研究最多的缀合蛋白之一。在这里，我们报告的电化学战略调查CYT的电活性Ç及其类似物具有破坏血红素部分，我。e。脱血红素细胞Ç（acyt Ç）和卟啉色素Ç（pcyt Ç）。电化学数据补充有低温和自旋探针电子顺磁共振（EPR）光谱。本报告的主要贡献是对cyt c的综合评估在一次电化学扫描中，在表面定位的氨基酸残基和血红素部分上还原和氧化。cyt c的电化学模式与类似物acyt c和pcyt c都大不相同，这可用于进一步研究细胞色素和其他血红蛋白的氧化还原特性和结构稳定性。