Modeling three-dimensional structure of two closely related Ni–Fe hydrogenases

The results of homology modeling of HydSL, a NiFe-hydrogenase from purple sulfur bacterium Thiocapsa roseopersicina BBS, and deep-water bacterium Alteromonas macleodii deep ecotype are presented in this work. It is shown that the models have larger confidence level than earlier published ones; full-...

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Bibliographic Details
Published in:Photosynthesis research 2015-08, Vol.125 (1-2), p.341-353
Main Authors: Abdullatypov, A. V, Tsygankov, A. A
Format: Article
Language:English
Subjects:
Allochromatium vinosum
Alteromonas - enzymology
Alteromonas macleodii
Amino acids
Bacteria
Biochemistry
Biomedical and Life Sciences
Desulfovibrio vulgaris
ecotypes
Enzymes
ferredoxin hydrogenase
Hydrogenase - chemistry
hydrophobicity
Life Sciences
Models, Molecular
Models, Structural
Oxidation-Reduction
oxygen
Oxygen - chemistry
Photosynthesis
Plant Genetics and Genomics
Plant Physiology
Plant Sciences
Regular Paper
Sulfur - chemistry
Sulfur compounds
thermal stability
Thiocapsa roseopersicina
Thiocapsa roseopersicina - enzymology
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Summary:The results of homology modeling of HydSL, a NiFe-hydrogenase from purple sulfur bacterium Thiocapsa roseopersicina BBS, and deep-water bacterium Alteromonas macleodii deep ecotype are presented in this work. It is shown that the models have larger confidence level than earlier published ones; full-size models of these enzymes are presented for the first time. The C-end fragment of small subunit of T. roseopersicina hydrogenase is shown to have random orientation in relation to the main protein globule. The obtained models of this enzyme have a large number of ion pairs, as well as thermostable HydSL hydrogenase from Allochromatium vinosum, in contrast to thermostable HydSL hydrogenase from Alt. macleodii and thermolabile HydAB hydrogenase from Desulfovibrio vulgaris. The possible determinant of oxygen stability of studied hydrogenases could be the lack of several intramolecular tunnels. Hydrophobic and electrostatic surfaces were mapped in order to find out possible pathways of coupling hydrogenase to electron-transferring chains, as well as methods for construction of artificial photobiohydrogen-producing systems.
ISSN:0166-8595
1573-5079
DOI:10.1007/s11120-014-0071-z