维持生命（呼吸）、细胞死亡（细胞凋亡）、氧气传输和免疫是血红素蛋白的主要生物功能。这些功能受血红素组中铁离子的轴向配体和氧化还原状态（在Fe2+和Fe3+之间的振荡）控制。本文旨在评估关于血红素蛋白中氧化和氧化对作用的当前知识状态。我们使用紫外-可见电子吸收光谱、拉曼光谱和拉曼成像技术，确定了全血中铁离子的氧化还原状态（未添加和添加抗凝剂）、红细胞中的血红蛋白、人类肺癌细胞线粒体中的细胞色素c以及分离的细胞色素c中的光谱。在这里，我们讨论Q电子吸收带光谱行为（即其分裂）和其消光系数的变化，以及氧化和氧化作用对振动的影响的机制。我们比较了人类红细胞血红蛋白和人类肺癌细胞线粒体中细胞色素c的血红素的氧化还原状态。提供的结果允许同时鉴定氧合血红蛋白和脱氧血红蛋白，其中1547和1604 cm-1振动对应于脱氧血红蛋白，1585和1638 cm-1分别对应于氧合血红蛋白。我们的结果扩展了对血红素蛋白中氧化和氧化作用的了解。我们实验证明了Q带分裂的电子-振动耦合机制。提供的结果扩展了对血红素蛋白中氧化和氧化作用的认识，并提供了两个过程强烈耦合的证据。我们表明视黄酸影响肺癌细胞线粒体中细胞色素c的血红蛋白的氧化还原状态。细胞色素c在线粒体中由氧化形式向还原形式的转变对线粒体功能障碍产生严重后果，从而抑制呼吸、细胞凋亡和细胞因子诱导。© 2023. Springer Nature Limited.

Maintaining life (respiration), cell death (apoptosis), oxygen transport and immunity are main biological functions of heme containing proteins. These functions are controlled by the axial ligands and the redox status of the iron ion (oscillations between Fe2+ and Fe3+) in the heme group. This paper aims to evaluate the current state of knowledge on oxidation and oxygenation effects in heme proteins. We determined the redox status of the iron ion in whole blood (without and with anticoagulant), hemoglobin in erythrocytes, in isolated cytochrome c and cytochrome c in mitochondria of the human lung cancer cells using UV-VIS electronic absorption spectroscopy, Raman spectroscopy and Raman imaging. Here we discussed the mechanism responsible for the Q electronic absorption band spectral behavior, i.e., its splitting, and its change in extinction coefficient, as well as vibrational modifications upon oxygenation and oxidation. We compared the redox status of heme in hemoglobin of human erythrocytes and cytochrome c in mitochondria of human lung cancer cells. Presented results allow simultaneous identification of oxy- and deoxy-Hb, where 1547 and 1604 cm-1 vibrations correspond to deoxygenated hemoglobin, while 1585 and 1638 cm-1 correspond to oxyhemoglobin, respectively. Our results extend knowledge of oxidation and oxygenation effects in heme proteins. We demonstrated experimentally the mechanism of electronic-vibrational coupling for the Q band splitting. Presented results extend knowledge on oxidation and oxygenation effects in heme proteins and provide evidence that both processes are strongly coupled. We showed that retinoic acid affects the redox state of heme in cytochrome c in mitochondria. The change of the redox status of cytochrome c in mitochondria from the oxidized form to the reduced form has very serious consequences in dysfunction of mitochondria resulting in inhibition of respiration, apoptosis and cytokine induction.© 2023. Springer Nature Limited.