Journal
JOURNAL OF BIOCHEMISTRY
Volume 159, Issue 5, Pages 527-538Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvv133
Keywords
copper; electron transfer; enzyme; serial femtosecond crystallography; X-ray free-electron laser
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Funding
- X-ray Free-Electron Laser Priority Strategy Program of the Ministry of Education, Culture, Sports, Science and Technology in Japan (MEXT)
- MEXT
- JSPS KAKENHI [15K18487]
- [254626]
- Grants-in-Aid for Scientific Research [16H06294, 26440028, 15K18487] Funding Source: KAKEN
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Serial femtosecond crystallography (SFX) has enabled the damage-free structural determination of metalloenzymes and filled the gaps of our knowledge between crystallographic and spectroscopic data. Crystallographers, however, scarcely know whether the rising technique provides truly new structural insights into mechanisms of metalloenzymes partly because of limited resolutions. Copper nitrite reductase (CuNiR), which converts nitrite to nitric oxide in denitrification, has been extensively studied by synchrotron radiation crystallography (SRX). Although catalytic Cu (Type 2 copper (T2Cu)) of CuNiR had been suspected to tolerate X-ray photoreduction, we here showed that T2Cu in the form free of nitrite is reduced and changes its coordination structure in SRX. Moreover, we determined the completely oxidized CuNiR structure at 1.43 angstrom resolution with SFX. Comparison between the high-resolution SFX and SRX data revealed the subtle structural change of a catalytic His residue by X-ray photoreduction. This finding, which SRX has failed to uncover, provides new insight into the reaction mechanism of CuNiR.
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