Reengineering cyt b562 for hydrogen production: A facile route to artificial hydrogenases

Dayn Joseph Sommer, Michael David Vaughn, Brett Colby Clark, John Tomlin, Anindya Roy, Giovanna Ghirlanda

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)598-603
Number of pages6
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1857
Issue number5
DOIs
Publication statusPublished - May 1 2016

Fingerprint

Hydrogenase
Reengineering
Hydrogen production
Hydrogen
Protons
Proteins
Catalysts
Organometallics
Cytochromes
Atmosphere
Aspartic Acid
Alanine
Methionine
Energy Metabolism
Oxidation-Reduction
Catalytic Domain
Tuning
Metals
protoporphyrin IX

Keywords

  • Cobalt catalysts
  • Fuel production
  • Protein engineering
  • Redox chemistry

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

Cite this

Reengineering cyt b562 for hydrogen production : A facile route to artificial hydrogenases. / Sommer, Dayn Joseph; Vaughn, Michael David; Clark, Brett Colby; Tomlin, John; Roy, Anindya; Ghirlanda, Giovanna.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1857, No. 5, 01.05.2016, p. 598-603.

Research output: Contribution to journalArticle

Sommer, Dayn Joseph ; Vaughn, Michael David ; Clark, Brett Colby ; Tomlin, John ; Roy, Anindya ; Ghirlanda, Giovanna. / Reengineering cyt b562 for hydrogen production : A facile route to artificial hydrogenases. In: Biochimica et Biophysica Acta - Bioenergetics. 2016 ; Vol. 1857, No. 5. pp. 598-603.
@article{86562ffbb36a4c948431aa2ec2adf1b6,
title = "Reengineering cyt b562 for hydrogen production: A facile route to artificial hydrogenases",
abstract = "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.",
keywords = "Cobalt catalysts, Fuel production, Protein engineering, Redox chemistry",
author = "Sommer, {Dayn Joseph} and Vaughn, {Michael David} and Clark, {Brett Colby} and John Tomlin and Anindya Roy and Giovanna Ghirlanda",
year = "2016",
month = "5",
day = "1",
doi = "10.1016/j.bbabio.2015.09.001",
language = "English",
volume = "1857",
pages = "598--603",
journal = "Biochimica et Biophysica Acta - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "5",

}

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

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

VL - 1857

SP - 598

EP - 603

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 5

ER -