Generating dihydrogen by tethering an [FeFe]hydrogenase via a molecular wire to the A1A/A1B sites of photosystem I

Research output: Contribution to journalArticle

Abstract

Photosystem I complexes from the menB deletion mutant of Synechocystis sp. PCC 6803 were previously wired to a Pt nanoparticle via a molecular wire consisting of 15-(3-methyl-1,4-naphthoquinone-2-yl)]pentadecyl sulfide. In the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-Pt nanoconstruct generated dihydrogen at a rate of 44.3 µmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. The menB deletion strain contains an interruption in the biosynthetic pathway of phylloquinone, which results in the presence of a displaceable plastoquinone-9 in the A1A/A1B sites. The synthesized quinone contains a headgroup identical to the native phylloquinone along with a 15-carbon long tail that is terminated in a thiol. The thiol on the molecular wire is used to bind the Pt nanoparticle. In this short communication, we replaced the Pt nanoparticle with an [FeFe]H2ase variant from Clostridium acetobutylicum that contains an exposed iron on the distal [4Fe-4S] cluster afforded by mutating the surface exposed Cys97 residue to Gly. The thiol on the molecular wire is then used to coordinate the corner iron atom of the iron–sulfur cluster. When all three components are combined and illuminated in the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct generated dihydrogen at a rate of 50.3 ± 9.96 μmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. This successful in vitro experiment sets the stage for assembling a PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct in vivo in the menB mutant of Synechocystis sp. PCC 6803.

Original languageEnglish (US)
JournalPhotosynthesis research
DOIs
StateAccepted/In press - Jan 1 2019

Fingerprint

nanowires
Photosystem I Protein Complex
Hydrogenase
photosystem I
nanoparticles
thiols
Sulfhydryl Compounds
Nanoparticles
Vitamin K 1
Synechocystis sp. PCC 6803
Synechocystis
phylloquinone
Wire
Electron Transport
Lighting
electron transfer
lighting
Iron
Clostridium acetobutylicum
Plastoquinone

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Plant Science
  • Cell Biology

Cite this

@article{d726f2163860452f8a8e53bc00c02b0e,
title = "Generating dihydrogen by tethering an [FeFe]hydrogenase via a molecular wire to the A1A/A1B sites of photosystem I",
abstract = "Photosystem I complexes from the menB deletion mutant of Synechocystis sp. PCC 6803 were previously wired to a Pt nanoparticle via a molecular wire consisting of 15-(3-methyl-1,4-naphthoquinone-2-yl)]pentadecyl sulfide. In the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-Pt nanoconstruct generated dihydrogen at a rate of 44.3 µmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. The menB deletion strain contains an interruption in the biosynthetic pathway of phylloquinone, which results in the presence of a displaceable plastoquinone-9 in the A1A/A1B sites. The synthesized quinone contains a headgroup identical to the native phylloquinone along with a 15-carbon long tail that is terminated in a thiol. The thiol on the molecular wire is used to bind the Pt nanoparticle. In this short communication, we replaced the Pt nanoparticle with an [FeFe]H2ase variant from Clostridium acetobutylicum that contains an exposed iron on the distal [4Fe-4S] cluster afforded by mutating the surface exposed Cys97 residue to Gly. The thiol on the molecular wire is then used to coordinate the corner iron atom of the iron–sulfur cluster. When all three components are combined and illuminated in the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct generated dihydrogen at a rate of 50.3 ± 9.96 μmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. This successful in vitro experiment sets the stage for assembling a PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct in vivo in the menB mutant of Synechocystis sp. PCC 6803.",
author = "Michael Gorka and Golbeck, {John H.}",
year = "2019",
month = "1",
day = "1",
doi = "10.1007/s11120-019-00685-y",
language = "English (US)",
journal = "Photosynthesis Research",
issn = "0166-8595",
publisher = "Springer Netherlands",

}

TY - JOUR

T1 - Generating dihydrogen by tethering an [FeFe]hydrogenase via a molecular wire to the A1A/A1B sites of photosystem I

AU - Gorka, Michael

AU - Golbeck, John H.

PY - 2019/1/1

Y1 - 2019/1/1

N2 - Photosystem I complexes from the menB deletion mutant of Synechocystis sp. PCC 6803 were previously wired to a Pt nanoparticle via a molecular wire consisting of 15-(3-methyl-1,4-naphthoquinone-2-yl)]pentadecyl sulfide. In the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-Pt nanoconstruct generated dihydrogen at a rate of 44.3 µmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. The menB deletion strain contains an interruption in the biosynthetic pathway of phylloquinone, which results in the presence of a displaceable plastoquinone-9 in the A1A/A1B sites. The synthesized quinone contains a headgroup identical to the native phylloquinone along with a 15-carbon long tail that is terminated in a thiol. The thiol on the molecular wire is used to bind the Pt nanoparticle. In this short communication, we replaced the Pt nanoparticle with an [FeFe]H2ase variant from Clostridium acetobutylicum that contains an exposed iron on the distal [4Fe-4S] cluster afforded by mutating the surface exposed Cys97 residue to Gly. The thiol on the molecular wire is then used to coordinate the corner iron atom of the iron–sulfur cluster. When all three components are combined and illuminated in the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct generated dihydrogen at a rate of 50.3 ± 9.96 μmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. This successful in vitro experiment sets the stage for assembling a PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct in vivo in the menB mutant of Synechocystis sp. PCC 6803.

AB - Photosystem I complexes from the menB deletion mutant of Synechocystis sp. PCC 6803 were previously wired to a Pt nanoparticle via a molecular wire consisting of 15-(3-methyl-1,4-naphthoquinone-2-yl)]pentadecyl sulfide. In the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-Pt nanoconstruct generated dihydrogen at a rate of 44.3 µmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. The menB deletion strain contains an interruption in the biosynthetic pathway of phylloquinone, which results in the presence of a displaceable plastoquinone-9 in the A1A/A1B sites. The synthesized quinone contains a headgroup identical to the native phylloquinone along with a 15-carbon long tail that is terminated in a thiol. The thiol on the molecular wire is used to bind the Pt nanoparticle. In this short communication, we replaced the Pt nanoparticle with an [FeFe]H2ase variant from Clostridium acetobutylicum that contains an exposed iron on the distal [4Fe-4S] cluster afforded by mutating the surface exposed Cys97 residue to Gly. The thiol on the molecular wire is then used to coordinate the corner iron atom of the iron–sulfur cluster. When all three components are combined and illuminated in the presence of a sacrificial electron donor and an electron transport mediator, the PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct generated dihydrogen at a rate of 50.3 ± 9.96 μmol of H2 mg Chl−1 h−1 during illumination at pH 8.3. This successful in vitro experiment sets the stage for assembling a PS I-NQ(CH2)15S-[FeFe]H2ase nanoconstruct in vivo in the menB mutant of Synechocystis sp. PCC 6803.

UR - http://www.scopus.com/inward/record.url?scp=85074697519&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85074697519&partnerID=8YFLogxK

U2 - 10.1007/s11120-019-00685-y

DO - 10.1007/s11120-019-00685-y

M3 - Article

C2 - 31673863

AN - SCOPUS:85074697519

JO - Photosynthesis Research

JF - Photosynthesis Research

SN - 0166-8595

ER -