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Title: Terminal Hydride Species in [FeFe]-Hydrogenases are Vibrationally Coupled to the Active Site Environment

Abstract

Here, a combination of NRVS and FT-IR spectroscopies and DFT calculations was used to observe and characterize Fe-H/D bending modes in CrHydA1 [FeFe]-hydrogenase Cys-to-Ser variant C169S. Mutagenesis of cysteine to serine at position 169 changes the functional group adjacent to the H-cluster from a -SH to -OH, thus altering the proton transfer pathway. C169S has a significant reduction in catalytic activity compared to the native CrHydA1, presumably due to less efficient transfer of protons to the H-cluster. This mutation allowed effective capture of a hydride/deuteride intermediate and facilitated direct detection of the Fe-H/D normal modes. We find a significant shift to higher frequency in a Fe-H bending mode of the C169S variant, as compared to previous findings with reconstituted native and oxadithiolate (ODT) substituted CrHydA1. Rationalized by DFT calculations, we propose that this shift is caused by a stronger interaction between the -OH of C169S with the bridgehead -NH- of the active site, as compared to the -SH of C169 in the native enzyme.

Authors:
 [1];  [1];  [2];  [3];  [2];  [2];  [1];  [1];  [4];  [5];  [5];  [6];  [6]
  1. Univ. of California, Davis, CA (United States)
  2. National Renewable Energy Lab. (NREL), Golden, CO (United States)
  3. Technische Univ. Berlin, Berlin (Germany)
  4. Argonne National Lab. (ANL), Argonne, IL (United States)
  5. Argonne National Lab. (ANL), Lemont, IL (United States)
  6. JASRI (Japan)
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1458904
Alternate Identifier(s):
OSTI ID: 1461219; OSTI ID: 1480684
Report Number(s):
NREL/JA-2700-71499
Journal ID: ISSN 1433-7851
Grant/Contract Number:  
AC36-08GO28308; AC02-06CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Angewandte Chemie (International Edition)
Additional Journal Information:
Journal Name: Angewandte Chemie (International Edition); Journal Volume: 57; Journal Issue: 33; Journal ID: ISSN 1433-7851
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; hydrogenase; NRVS; FTIR; synchrotron radiation

Citation Formats

Cramer, Stephen Paul, Pham, Cindy C., Mulder, David W., Pelmenschikov, Vladimir, King, Paul W., Ratzloff, Michael W., Wang, Hongxin, Mishra, Nakul, Alp, Ercan, Zhao, Jiyong, Hu, Michael Y., Tamasaku, Kenji, and Yoda, Yoshitaka. Terminal Hydride Species in [FeFe]-Hydrogenases are Vibrationally Coupled to the Active Site Environment. United States: N. p., 2018. Web. doi:10.1002/anie.201805144.
Cramer, Stephen Paul, Pham, Cindy C., Mulder, David W., Pelmenschikov, Vladimir, King, Paul W., Ratzloff, Michael W., Wang, Hongxin, Mishra, Nakul, Alp, Ercan, Zhao, Jiyong, Hu, Michael Y., Tamasaku, Kenji, & Yoda, Yoshitaka. Terminal Hydride Species in [FeFe]-Hydrogenases are Vibrationally Coupled to the Active Site Environment. United States. doi:10.1002/anie.201805144.
Cramer, Stephen Paul, Pham, Cindy C., Mulder, David W., Pelmenschikov, Vladimir, King, Paul W., Ratzloff, Michael W., Wang, Hongxin, Mishra, Nakul, Alp, Ercan, Zhao, Jiyong, Hu, Michael Y., Tamasaku, Kenji, and Yoda, Yoshitaka. Tue . "Terminal Hydride Species in [FeFe]-Hydrogenases are Vibrationally Coupled to the Active Site Environment". United States. doi:10.1002/anie.201805144. https://www.osti.gov/servlets/purl/1458904.
@article{osti_1458904,
title = {Terminal Hydride Species in [FeFe]-Hydrogenases are Vibrationally Coupled to the Active Site Environment},
author = {Cramer, Stephen Paul and Pham, Cindy C. and Mulder, David W. and Pelmenschikov, Vladimir and King, Paul W. and Ratzloff, Michael W. and Wang, Hongxin and Mishra, Nakul and Alp, Ercan and Zhao, Jiyong and Hu, Michael Y. and Tamasaku, Kenji and Yoda, Yoshitaka},
abstractNote = {Here, a combination of NRVS and FT-IR spectroscopies and DFT calculations was used to observe and characterize Fe-H/D bending modes in CrHydA1 [FeFe]-hydrogenase Cys-to-Ser variant C169S. Mutagenesis of cysteine to serine at position 169 changes the functional group adjacent to the H-cluster from a -SH to -OH, thus altering the proton transfer pathway. C169S has a significant reduction in catalytic activity compared to the native CrHydA1, presumably due to less efficient transfer of protons to the H-cluster. This mutation allowed effective capture of a hydride/deuteride intermediate and facilitated direct detection of the Fe-H/D normal modes. We find a significant shift to higher frequency in a Fe-H bending mode of the C169S variant, as compared to previous findings with reconstituted native and oxadithiolate (ODT) substituted CrHydA1. Rationalized by DFT calculations, we propose that this shift is caused by a stronger interaction between the -OH of C169S with the bridgehead -NH- of the active site, as compared to the -SH of C169 in the native enzyme.},
doi = {10.1002/anie.201805144},
journal = {Angewandte Chemie (International Edition)},
number = 33,
volume = 57,
place = {United States},
year = {2018},
month = {6}
}

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