TY - JOUR
T1 - Reengineering cyt b562 for hydrogen production
T2 - A facile route to artificial hydrogenases
AU - Sommer, Dayn Joseph
AU - Vaughn, Michael David
AU - Clark, Brett Colby
AU - Tomlin, John
AU - Roy, Anindya
AU - Ghirlanda, Giovanna
N1 - Publisher Copyright:
© 2015 Elsevier B.V. All rights reserved.
PY - 2016/5/1
Y1 - 2016/5/1
N2 - Bioinspired, protein-based molecular catalysts utilizing base metals at the active are emerging as a promising avenue to sustainable hydrogen production. The protein matrix modulates the intrinsic reactivity of organometallic active sites by tuning second-sphere and long-range interactions. Here, we show that swapping Co-Protoporphyrin IX for Fe-Protoporphyrin IX in cytochrome b562 results in an efficient catalyst for photoinduced proton reduction to molecular hydrogen. Further, the activity of wild type Co-cyt b562 can be modulated by a factor of 2.5 by exchanging the coordinating methionine with alanine or aspartic acid. The observed turnover numbers (TON) range between 125 and 305, and correlate well with the redox potential of the Co-cyt b562 mutants. The photosensitized system catalyzes proton reduction with high efficiency even under an aerobic atmosphere, implicating its use for biotechnological applications. This article is part of a Special Issue entitled Biodesign for Bioenergetics - the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.
AB - Bioinspired, protein-based molecular catalysts utilizing base metals at the active are emerging as a promising avenue to sustainable hydrogen production. The protein matrix modulates the intrinsic reactivity of organometallic active sites by tuning second-sphere and long-range interactions. Here, we show that swapping Co-Protoporphyrin IX for Fe-Protoporphyrin IX in cytochrome b562 results in an efficient catalyst for photoinduced proton reduction to molecular hydrogen. Further, the activity of wild type Co-cyt b562 can be modulated by a factor of 2.5 by exchanging the coordinating methionine with alanine or aspartic acid. The observed turnover numbers (TON) range between 125 and 305, and correlate well with the redox potential of the Co-cyt b562 mutants. The photosensitized system catalyzes proton reduction with high efficiency even under an aerobic atmosphere, implicating its use for biotechnological applications. This article is part of a Special Issue entitled Biodesign for Bioenergetics - the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.
KW - Cobalt catalysts
KW - Fuel production
KW - Protein engineering
KW - Redox chemistry
UR - http://www.scopus.com/inward/record.url?scp=84964063480&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84964063480&partnerID=8YFLogxK
U2 - 10.1016/j.bbabio.2015.09.001
DO - 10.1016/j.bbabio.2015.09.001
M3 - Article
C2 - 26375327
AN - SCOPUS:84964063480
SN - 0005-2728
VL - 1857
SP - 598
EP - 603
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 5
ER -