S2/2 Structure and function of photosynthetic membrane proteins

Fromme, Petra; Yu, Hualiang; Fromme, Raimund; Chauhan, Devendra Kumar; Varco-Merth, Ben; Lawrence, Robert; DeRuyter, Yana S.; Jolley, Craig C.; Thangaraj, Balakumar; Vanselow, Christopher; Grotjohann, Ingo; Bottin, Hervé; Sétif, Pièrre

doi:10.1016/j.bbabio.2008.05.089

Cited by 1 publication

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“…The combined activity of PSII, PSI, and the electron transfer chain (ETC) results in the reduction of NADP + and the transfer of protons across the thylakoid membrane. The translocated protons drive ATP synthesis via ATP synthase and the resultant ATP and NADPH drive CO 2 fixation through the Calvin cycle. , …”

Section: Introductionmentioning

confidence: 99%

“…The translocated protons drive ATP synthesis via ATP synthase and the resultant ATP and NADPH drive CO 2 fixation through the Calvin cycle. 14,15 PSI accomplishes the unique biological function of converting solar energy into reducing power, and as such has been intensely researched as an alternative energy solution. Greenbaum et al demonstrated that PSI vectorial arrays prepared on derivatized gold surfaces could function as a biomolecular photovoltaic device, and furthermore that the nature of the derivatized surface (i.e., negative, positive, or hydrophilic) influenced PSI orientation.…”

Section: ■ Introductionmentioning

confidence: 99%

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Structure and Function of Photosystem I–[FeFe] Hydrogenase Protein Fusions: An All-Atom Molecular Dynamics Study

Harris

Cheng

Frymier³

2016

J. Phys. Chem. B

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All-atom molecular dynamics (MD) simulation was used to study the solution dynamics and protein-protein interactions of protein fusions of photosystem I (PSI) from Thermosynechococcus elongatus and an [FeFe]-hydrogenase (FeFe H2ase) from Clostridium pasteurianum, a unique complex capable of photocatalytic hydrogen production. This study involved fusions of these two proteins via dithiol linkers of different length including decanedithiol, octanedithiol, and hexanedithiol, for which experimental data had previously been obtained. Evaluation of root-mean-squared deviations (RMSDs) relative to the respective crystal structures of PSI and the FeFe H2ase shows that these fusion complexes approach stable equilibrium conformations during the MD simulations. Investigating protein mobility via root-mean-squared fluctuations (RMSFs) reveals that tethering via the shortest hexanedithiol linker results in increased atomic fluctuations of both PSI and the hydrogenase in these fusion complexes. Evaluation of the inter- and intraprotein electron transfer distances in these fusion complexes indicates that the structural changes in the FeFe H2ase arising from ligation to PSI via the shortest hexanedithiol linker may hinder electron transport in the hydrogenase, thus providing a molecular level explanation for the observation that the medium-length octanedithiol linker gives the highest hydrogen production rate.

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Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%