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Probing Substrate T...
Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis : An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase
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- Cabotaje, Princess R. (författare)
- Uppsala universitet,Molekylär biomimetik
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- Walter, Kaija (författare)
- Uppsala universitet,Molekylär biomimetik
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- Zamader, Afridi (författare)
- Uppsala universitet,Molekylär biomimetik
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- Huang, Ping (författare)
- Uppsala universitet,Molekylär biomimetik
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- Ho, Felix M. (författare)
- Uppsala universitet,Molekylär biomimetik
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- Land, Henrik (författare)
- Uppsala universitet,Molekylär biomimetik
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- Senger, Moritz (författare)
- Uppsala universitet,Fysikalisk kemi
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- Berggren, Gustav (författare)
- Uppsala universitet,Molekylär biomimetik
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(creator_code:org_t)
- American Chemical Society (ACS), 2023
- 2023
- Engelska.
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Ingår i: ACS Catalysis. - : American Chemical Society (ACS). - 2155-5435. ; 13:15, s. 10435-10446
- Relaterad länk:
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https://doi.org/10.1...
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https://uu.diva-port... (primary) (Raw object)
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- [FeFe] hydrogenases, metalloenzymes catalyzing proton/dihydrogeninterconversion, have attracted intense attention due to their remarkablecatalytic properties and (bio-)technological potential for a futurehydrogen economy. In order to unravel the factors enabling their efficientcatalysis, both their unique organometallic cofactors and proteinstructural features, i.e., "outer-coordination sphere"effects have been intensively studied. These structurally diverseenzymes are divided into distinct phylogenetic groups, denoted asGroup A-D. Prototypical Group A hydrogenases display high turnoverrates (10(4)-10(5) s(-1)).Conversely, the sole characterized Group D representative, Thermoanaerobacter mathranii HydS (TamHydS), shows relatively low catalytic activity (specific activity10(-1) & mu;mol H-2 mg(-1) min(-1)) and has been proposed to serve a H-2-sensory function. The various groups of [FeFe] hydrogenaseshare the same catalytic cofactor, the H-cluster, and the structuralfactors causing the diverging reactivities of Group A and D remainto be elucidated. In the case of the highly active Group A enzymes,a well-defined proton transfer pathway (PTP) has been identified,which shuttles H+ between the enzyme surface and the activesite. In Group D hydrogenases, this conserved pathway is absent. Here,we report on the identification of highly conserved amino acid residuesin Group D hydrogenases that constitute a possible alternative PTP.We varied two proposed key amino acid residues of this pathway (E252and E289, TamHydS numbering) via site-directed mutagenesisand analyzed the resulting variants via biochemical and spectroscopicmethods. All variants displayed significantly decreased H-2-evolution and -oxidation activities. Additionally, the variantsshowed two redox states that were not characterized previously. Thesefindings provide initial evidence that these amino acid residues arecentral to the putative PTP of Group D [FeFe] hydrogenase. Since theidentified residues are highly conserved in Group D exclusively, ourresults support the notion that the PTP is not universal for differentphylogenetic groups in [FeFe] hydrogenases.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- hydrogenases
- hydrogen
- substrate transport
- redox catalysis
- bioinorganic chemistry
- enzymecatalysis
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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