Hydrogenase enzymes produce H2gas, which can be a potential source of alternative energy. Inspired by the [NiFe] hydrogenases, we report the construction of a de novo‐designed artificial hydrogenase (ArH). The ArH is a dimeric coiled coil where two cysteine (Cys) residues are introduced at tandem
- Home
- Search Results
- Page 1 of 1
Search for: All records
-
Total Resources1
- Resource Type
-
00010
- Availability
-
10
- Author / Contributor
- Filter by Author / Creator
-
-
Chakraborty, Saumen (1)
-
Hammer, Nathan I. (1)
-
Hunt, Leigh Anna (1)
-
Malayam Parambath, Sreya (1)
-
Selvan, Dhanashree (1)
-
Williams, Ashley E. (1)
-
#Tyler Phillips, Kenneth E. (0)
-
#Willis, Ciara (0)
-
& Abreu-Ramos, E. D. (0)
-
& Abramson, C. I. (0)
-
& Abreu-Ramos, E. D. (0)
-
& Adams, S.G. (0)
-
& Ahmed, K. (0)
-
& Ahmed, Khadija. (0)
-
& Akcil-Okan, O. (0)
-
& Akuom, D. (0)
-
& Aleven, V. (0)
-
& Andrews-Larson, C. (0)
-
& Archibald, J. (0)
-
& Arnett, N. (0)
-
- Filter by Editor
-
-
& Spizer, S. M. (0)
-
& . Spizer, S. (0)
-
& Ahn, J. (0)
-
& Bateiha, S. (0)
-
& Bosch, N. (0)
-
& Brennan K. (0)
-
& Brennan, K. (0)
-
& Chen, B. (0)
-
& Chen, Bodong (0)
-
& Drown, S. (0)
-
& Ferretti, F. (0)
-
& Higgins, A. (0)
-
& J. Peters (0)
-
& Kali, Y. (0)
-
& Ruiz-Arias, P.M. (0)
-
& S. Spitzer (0)
-
& Spitzer, S. (0)
-
& Spitzer, S.M. (0)
-
(submitted - in Review for IEEE ICASSP-2024) (0)
-
- (0)
-
-
Have feedback or suggestions for a way to improve these results?
!
Note: When clicking on a Digital Object Identifier (DOI) number, you will be taken to an external site maintained by the publisher.
Some full text articles may not yet be available without a charge during the embargo (administrative interval).
What is a DOI Number?
Some links on this page may take you to non-federal websites. Their policies may differ from this site.
-
Abstract a /d positions of a heptad to create a tetrathiolato Ni binding site. Spectroscopic studies show that Ni binding significantly stabilizes the peptide producing electronic transitions characteristic of Ni‐thiolate proteins. The ArH produces H2photocatalytically, demonstrating a bell‐shaped pH‐dependence on activity. Fluorescence lifetimes and transient absorption spectroscopic studies are undertaken to elucidate the nature of pH‐dependence, and to monitor the reaction kinetics of the photochemical processes. pH titrations are employed to determine the role of protonated Cys on reactivity. Through combining these results, a fine balance is found between solution acidity and the electron transfer steps. This balance is critical to maximize the production of NiI‐peptide and protonation of the NiII−H−intermediate (Ni−R) by a Cys (pK a≈6.4) to produce H2.