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Title: Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation

Authors:
; ; ; ; ; ; ; ; ; ORCiD logo
Publication Date:
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1363692
Grant/Contract Number:
FG02-10ER16194
Resource Type:
Journal Article: Published Article
Journal Name:
Biochemistry
Additional Journal Information:
Related Information: CHORUS Timestamp: 2018-05-19 09:18:39; Journal ID: ISSN 0006-2960
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English

Citation Formats

Shepard, Eric M., Byer, Amanda S., Aggarwal, Priyanka, Betz, Jeremiah N., Scott, Anna G., Shisler, Krista A., Usselman, Robert J., Eaton, Gareth R., Eaton, Sandra S., and Broderick, Joan B. Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation. United States: N. p., 2017. Web. doi:10.1021/acs.biochem.7b00169.
Shepard, Eric M., Byer, Amanda S., Aggarwal, Priyanka, Betz, Jeremiah N., Scott, Anna G., Shisler, Krista A., Usselman, Robert J., Eaton, Gareth R., Eaton, Sandra S., & Broderick, Joan B. Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation. United States. doi:10.1021/acs.biochem.7b00169.
Shepard, Eric M., Byer, Amanda S., Aggarwal, Priyanka, Betz, Jeremiah N., Scott, Anna G., Shisler, Krista A., Usselman, Robert J., Eaton, Gareth R., Eaton, Sandra S., and Broderick, Joan B. Fri . "Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation". United States. doi:10.1021/acs.biochem.7b00169.
@article{osti_1363692,
title = {Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation},
author = {Shepard, Eric M. and Byer, Amanda S. and Aggarwal, Priyanka and Betz, Jeremiah N. and Scott, Anna G. and Shisler, Krista A. and Usselman, Robert J. and Eaton, Gareth R. and Eaton, Sandra S. and Broderick, Joan B.},
abstractNote = {},
doi = {10.1021/acs.biochem.7b00169},
journal = {Biochemistry},
number = ,
volume = ,
place = {United States},
year = {Fri May 19 00:00:00 EDT 2017},
month = {Fri May 19 00:00:00 EDT 2017}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1021/acs.biochem.7b00169

Citation Metrics:
Cited by: 1work
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  • {sup 57}Fe, {sup 33}S, and {sup 14}N electron nuclear double resonance (ENDOR) studies have been performed to characterize the (4Fe-4S){sup {plus}} cluster at the active site of aconitase. Q-band {sup 57}Fe ENDOR of isotopically enriched enzyme, both substrate free and in the enzyme-substrate complex, reveals four inequivalent iron sites. In agreement with Mossbauer studies, one of the iron ions, Fe{sub a}, which is easily removed by oxidation to yield the (3Fe-4S){sup {plus}} cluster of inactive aconitase, shows a dramatic change in the presence of substrate. The remaining iron sites, Fe{sub b1,2,3,} show minor changes when substrate is bound. Methods devisedmore » by the authors for analyzing and simulating ENDOR spectra of a randomly oriented paramagnet have been used to determine the principal values and orientation relative to the g tensor for the hyperfine tensors of three of the four inequivalent iron sites of the (4Fe-4S){sup {plus}} cluster, Fe{sub a}, Fe{sub b2}, and Fe{sub b3}, in the substrate-free enzyme and the enzyme-substrate complex. {sup 33}S ENDOR data for the enzyme-substrate complex using enzyme reconstituted with {sup 33}S show that the four inorganic bridging sulfide ions of the (4Fe-4S){sup {plus}} cube have isotropic hyperfine couplings of A(S) < 12 MHz, and analysis indicates that they can be divided into two pairs, the analysis further places these pairs within the cube relative to the iron sites. {sup 33}S data for substrate-free enzyme is qualitatively similar and can be completely simulated by two types of S{sup 2{minus}} ion, with A(S1) {approximately} 7.5 and A(S2) {approximately} 9 MHz; the full hyperfine tensors have been determined.« less
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