Gorbikova Elena, Kalendar Ruslan
Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Department of Agricultural Sciences, University of Helsinki, Helsinki, Finland.
Front Chem. 2020 May 5;8:387. doi: 10.3389/fchem.2020.00387. eCollection 2020.
Cytochrome oxidase is terminal enzyme in the respiratory chain of mitochondria and many aerobic bacteria. It catalyzes reduction of oxygen to water. During its catalysis, CO proceeds through several quite stable intermediates (, , , , ). This work is concentrated on the elucidation of the differences between structures of oxidized intermediates and in different CO variants and at different pH values. Oxidized intermediates of wild type and mutated CO from were studied by means of static and time-resolved Fourier-transform infrared spectroscopy in acidic and alkaline conditions in the infrared region 1800-1000 cm. No reasonable differences were found between all variants in these conditions, and in this spectral region. This finding means that the binuclear center of oxygen reduction keeps a very similar structure and holds the same ligands in the studied conditions. The further investigation in search of differences should be performed in the 4000-2000 cm IR region where water ligands absorb.
细胞色素氧化酶是线粒体和许多需氧细菌呼吸链中的末端酶。它催化氧气还原为水。在其催化过程中，一氧化碳会经过几种相当稳定的中间体（，，，，）。这项工作集中于阐明不同一氧化碳变体以及在不同pH值下氧化中间体和的结构差异。通过在1800 - 1000厘米红外区域的酸性和碱性条件下进行静态和时间分辨傅里叶变换红外光谱研究，对来自的野生型和突变型一氧化碳的氧化中间体进行了研究。在这些条件下以及在该光谱区域内，所有变体之间未发现合理差异。这一发现意味着在所研究的条件下，氧还原的双核中心保持非常相似的结构并拥有相同的配体。应在水配体吸收的4000 - 2000厘米红外区域进行进一步研究以寻找差异。
