The Three-Dimensional Structure of [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Hildenborough: A Hydrogenase without a Bridging Ligand in the Active Site in Its Oxidised, “as-Isolated” State

H2‐Fueled ATP Synthesis on an Electrode: Mimicking Cellular Respiration

“…Figure 2 B illustrates the appearance of a hydrogenase monolayer with a surface roughness of 5 nm after its covalent binding to the gold surface modified with a self‐assembled monolayer (SAM) of 4‐aminothiophenol. This roughness corresponds to that expected for a monolayer of hydrogenase molecules considering the enzyme dimensions 18. Figure 2 C illustrates that fusion of the proteoliposomes containing ATPase smooths the underlying roughness, but shows protrusions corresponding to the membrane‐embedded ATPase.…”

Structural Foundations for O2 Sensitivity and O2 Tolerance in [NiFe]-Hydrogenases

“…In conclusion, although the exact identity of states like Ni-A and the oneelectron more reduced unready Ni-SU form ( Fig. 2.3b) is still debated, our interpretations seem to be compatible with all the discussed crystallographic, as well as with other experimental results, as previously reviewed by Fontecilla-Camps et al (2007) (Marques et al 2010).…”

“…Based on several sources (Brecht et al 2003;FontecillaCamps et al 2007;Pandelia et al 2010), a hydride is postulated to bridge the Ni and Fe ions in the active Ni-C form, replacing the hydroxide found in the Ni-B state. More recently, Marques et al (2010) have reported on the structure of the [NiFeSe]-hydrogenase from D. vulgaris Hildenborough. This structure contains a mixture of oxidized states and includes three different conformations for its SeCys residue.…”

Interaction of the active site of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough with carbon monoxide and oxygen inhibitors

“…This can be explained from the crystallographic data recently reported for D. vulgaris Ni-FeSe hydrogenase in the Ni-IS state [35], in which an extra sulphur atom binds Ni and Se leading to a conformation of the selenocysteine that should prevent extrinsic CO binding the Ni atom (Scheme 1b).…”