Journal article
Retuning the catalytic bias and overpotential of a [NiFe]-hydrogenase via a single amino acid exchange at the electron entry/exit site
- Abstract:
- The redox chemistry of the electron entry/exit site in Escherichia coli hydrogenase-1 is shown to play a vital role in tuning biocatalysis. Inspired by nature, we generate a HyaA-R193L variant to disrupt a proposed Arg-His cation-π interaction in the secondary coordination sphere of the outermost, "distal", iron-sulfur cluster. This rewires the enzyme, enhancing the relative rate of H2 production and the thermodynamic efficiency of H2 oxidation catalysis. On the basis of Fourier transformed alternating current voltammetry measurements, we relate these changes in catalysis to a shift in the distal [Fe4S4]2+/1+ redox potential, a previously experimentally inaccessible parameter. Thus, metalloenzyme chemistry is shown to be tuned by the second coordination sphere of an electron transfer site distant from the catalytic center.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Version of record, pdf, 2.3MB, Terms of use)
-
- Publisher copy:
- 10.1021/jacs.7b03611
Authors
+ Australian Research Council
More from this funder
- Funding agency for:
- Gavaghan, D
- Bond, A
- Parkin, A
- Grant:
- EP/I017909/1
- DP170101535
- DP170101535
+ University of York
More from this funder
- Funding agency for:
- Walton, J
- Parkin, A
- Grant:
- EP/M506394/1
- DP170101535
+ Engineering and Physical Sciences Research Council
More from this funder
- Funding agency for:
- Walton, J
- Gavaghan, D
- Roessler, M
- Grant:
- EP/M506394/1
- EP/I017909/1
- EP/M024393/1
+ Royal Society
More from this funder
- Funding agency for:
- Adamson, H
- Bond, A
- Parkin, A
- Grant:
- BB/F017316/1
- DP170101535
- DP170101535
- Publisher:
- American Chemical Society
- Journal:
- Journal of the American Chemical Society More from this journal
- Volume:
- 139
- Issue:
- 31
- Pages:
- 10677-10686
- Publication date:
- 2017-07-12
- Acceptance date:
- 2017-07-11
- DOI:
- EISSN:
-
1520-5126
- ISSN:
-
0002-7863
- Pmid:
-
28697596
- Language:
-
English
- Keywords:
- Pubs id:
-
pubs:708065
- UUID:
-
uuid:aaa5c831-ee6f-424e-adb7-3abd92046afb
- Local pid:
-
pubs:708065
- Source identifiers:
-
708065
- Deposit date:
-
2017-08-22
Terms of use
- Copyright holder:
- © 2017 American Chemical Society
- Copyright date:
- 2017
- Notes:
- This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record