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Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.

Research & information: general --- Biology, life sciences --- CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal–dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn–Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP—carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA—5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich’s ataxia --- n/a --- metal-dithiolene --- pseudo-Jahn-Teller effect --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- Friedreich's ataxia

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.

CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal–dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn–Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP—carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA—5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich’s ataxia --- n/a --- metal-dithiolene --- pseudo-Jahn-Teller effect --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- Friedreich's ataxia