6rp2
Threonine to Cysteine (T225C) variant of E coli hydrogenase-1
Structural highlights
FunctionMBHS_ECOLI This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. Publication Abstract from PubMedHydrogenase-1 (Hyd-1) from E. coli poses a conundrum regarding the properties of electrocatalytic reversibility and associated bidirectionality now established for many redox enzymes. Its excellent H2-oxidizing activity begins only once a substantial overpo-tential is applied, and it cannot produce H2. A major reason for its unidirectional behavior is that the reduction potentials of its electron-relaying FeS clusters are too positive relative to the 2H+/H2 couple at neutral pH; consequently, electrons held within the enzyme lack the energy to drive H2 production. However, Hyd-1 is O2-tolerant and even functions in air. Changing a tyrosine (Y) or threonine (T), located on the protein surface within 10 A of the distal [4Fe-4S] and medial [3Fe-4S] clusters, to cysteine (C), allows site-selective attachment of a silver nanocluster (AgNC), the reduced or photoexcited state of which is a powerful reduct-ant. The AgNC provides a new additional redox site, capturing externally-supplied electrons with sufficiently high energy to drive H2 production. Assemblies of Y'227C (or T'225C) with AgNCs/PMAA (PMAA = polymethylacrylate templating several AgNC) are also electroactive for H2 production at a TiO2 electrode. A colloidal system for visible-light photo-H2 generation is made by building the hybrid enzyme into a heterostructure with TiO2 and graphitic carbon nitride (g-C3N4), the resulting scaffold promoting uptake of electrons excited at the AgNC. Each hydrogenase produces 40 molecules of H2 per second and sustains 20% activity in air. Aerobic Photocatalytic H2 Production by a [NiFe] hydrogenase Engineered to Place a Silver Nanocluster in the Electron Relay.,Zhang L, Morello G, Carr SB, Armstrong FA J Am Chem Soc. 2020 Jun 24. doi: 10.1021/jacs.0c04302. PMID:32579353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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