RESUMO
Hydrogenases (H2 ases) are benchmark electrocatalysts for H2 production, both in biology and (photo)catalysis inâ vitro. We report the tailoring of a p-type Si photocathode for optimal loading and wiring of H2 ase through the introduction of a hierarchical inverse opal (IO) TiO2 interlayer. This proton-reducing Si|IO-TiO2 |H2 ase photocathode is capable of driving overall water splitting in combination with a photoanode. We demonstrate unassisted (bias-free) water splitting by wiring Si|IO-TiO2 |H2 ase to a modified BiVO4 photoanode in a photoelectrochemical (PEC) cell during several hours of irradiation. Connecting the Si|IO-TiO2 |H2 ase to a photosystemâ II (PSII) photoanode provides proof of concept for an engineered Z-scheme that replaces the non-complementary, natural light absorber photosystemâ I with a complementary abiotic silicon photocathode.
Assuntos
Hidrogenase/metabolismo , Energia Solar , Água/metabolismo , Bismuto/química , Técnicas Eletroquímicas , Eletrodos , Hidrogênio/metabolismo , Luz , Processos Fotoquímicos , Complexo de Proteína do Fotossistema II/química , Complexo de Proteína do Fotossistema II/metabolismo , Técnicas de Microbalança de Cristal de Quartzo , Silício/química , Titânio/química , Vanadatos/química , Água/químicaRESUMO
During photosynthesis, electrons are transferred between the cytochrome b6f complex and photosystem I. This is carried out by the protein plastocyanin in plant chloroplasts, or by either plastocyanin or cytochrome c6 in many cyanobacteria and eukaryotic algal species. There are three further cytochrome c6 homologs: cytochrome c6A in plants and green algae, and cytochromes c6B and c6C in cyanobacteria. The function of these proteins is unknown. Here, we present a comprehensive analysis of the evolutionary relationship between the members of the cytochrome c6 family in photosynthetic organisms. Our phylogenetic analyses show that cytochromes c6B and c6C are likely to be orthologs that arose from a duplication of cytochrome c6, but that there is no evidence for separate origins for cytochromes c6B and c6C. We therefore propose renaming cytochrome c6C as cytochrome c6B. We show that cytochrome c6A is likely to have arisen from cytochrome c6B rather than by an independent duplication of cytochrome c6, and present evidence for an independent origin of a protein with some of the features of cytochrome c6A in peridinin dinoflagellates. We conclude with a new comprehensive model of the evolution of the cytochrome c6 family which is an integral part of understanding the function of the enigmatic cytochrome c6 homologs.