Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.
Methanogens are microorganisms that produce methane as a metabolic byproduct in hypoxic conditions. They are prokaryotic and belong to the domain Archaea. All known methanogens are members of the archaeal phylum Euryarchaeota. Methanogens are common in wetlands, where they are responsible for marsh gas, and can occur in the digestive tracts of animals including ruminants and humans, where they are responsible for the methane content of belching and flatulence. In marine sediments, the biological production of methane, termed methanogenesis, is generally confined to where sulfates are depleted below the top layers. Methanogenic archaea populations play an indispensable role in anaerobic wastewater treatments. Other methanogens are extremophiles, found in environments such as hot springs and submarine hydrothermal vents as well as in the "solid" rock of Earth's crust, kilometers below the surface.
Nitrogenases are enzymes (EC 1.18.6.1EC 1.19.6.1) that are produced by certain bacteria, such as cyanobacteria (blue-green bacteria) and rhizobacteria. These enzymes are responsible for the reduction of nitrogen (N2) to ammonia (NH3). Nitrogenases are the only family of enzymes known to catalyze this reaction, which is a step in the process of nitrogen fixation. Nitrogen fixation is required for all forms of life, with nitrogen being essential for the biosynthesis of molecules (nucleotides, amino acids) that create plants, animals and other organisms. They are encoded by the Nif genes or homologs. They are related to protochlorophyllide reductase.
A hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2), as shown below:
Biohydrogen is H2 that is produced biologically. Interest is high in this technology because H2 is a clean fuel and can be readily produced from certain kinds of biomass, including biological waste. Furthermore some photosynthetic microorganisms are capable to produce H2 directly from water splitting using light as energy source.
Bioorganometallic chemistry is the study of biologically active molecules that contain carbon directly bonded to metals or metalloids. The importance of main-group and transition-metal centers has long been recognized as important to the function of enzymes and other biomolecules. However, only a small subset of naturally-occurring metal complexes and synthetically prepared pharmaceuticals are organometallic; that is, they feature a direct covalent bond between the metal(loid) and a carbon atom. The first, and for a long time, the only examples of naturally occurring bioorganometallic compounds were the cobalamin cofactors (vitamin B12) in its various forms. In the 21st century, discovery of new systems containing carbon-metal bonds in biology, bioorganometallic chemistry is rapidly emerging as a distinct subdiscipline of bioinorganic chemistry that straddles organometallic chemistry and biochemistry. Naturally occurring bioorganometallics include enzymes and sensor proteins. Also within this realm are synthetically prepared organometallic compounds that serve as new drugs and imaging agents (technetium-99m sestamibi) as well as the principles relevant to the toxicology of organometallic compounds (e.g., methylmercury). Consequently, bioorganometallic chemistry is increasingly relevant to medicine and pharmacology.
Tetrahydromethanopterin is a coenzyme in methanogenesis. It is the carrier of the C1 group as it is reduced to the methyl level, before transferring to the coenzyme M.
Coenzyme B is a coenzyme required for redox reactions in methanogens. The full chemical name of coenzyme B is 7-mercaptoheptanoylthreoninephosphate. The molecule contains a thiol, which is its principal site of reaction.
Methanofurans are a family of chemical compounds found in methanogenic archaea. These species feature a 2-aminomethylfuran linked to phenoxy group. At least three different end groups are recognized: R = tricarboxyheptanoyl (methanofuran), glutamyl-glutamyl, tricarboxy-2-hydroxyheptanoyl.
In enzymology, carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a coenzyme F420 hydrogenase (EC 1.12.98.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a cytochrome-c3 hydrogenase (EC 1.12.2.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a Methanosarcina-phenazine hydrogenase (EC 1.12.98.3) is an enzyme that catalyzes the chemical reaction
In enzymology, coenzyme-B sulfoethylthiotransferase, also known as methyl-coenzyme M reductase (MCR) or most systematically as 2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreonine S-(2-sulfoethyl)thiotransferase is an enzyme that catalyzes the final step in the formation of methane. It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. Via this enzyme, most of the natural gas on earth was produced. Ruminants produce methane because their rumens contain methanogenic prokaryotes (Archaea) that encode and express the set of genes of this enzymatic complex.
Coenzyme F420 or 8-hydroxy-5-deazaflavin is a coenzyme (sometimes called a cofactor) involved in redox reactions in methanogens, in many Actinomycetota, and sporadically in other bacterial lineages. It is a flavin derivative with an absorption maximum at 420 nm—hence its name. The coenzyme is a substrate for coenzyme F420 hydrogenase, 5,10-methylenetetrahydromethanopterin reductase and methylenetetrahydromethanopterin dehydrogenase.
Methanophenazine, a phenazine derivative, is a strongly hydrophobic redox-active cofactor with a role in electron transport in some methanogens. This chromophore can be purified from membranes of methanogenic archaea such as Methanosarcina mazei. The enzyme methanosarcina-phenazine hydrogenase has the name methanophenazine hydrogenase as a synonym.
Methanocaldococcus jannaschii is a thermophilic methanogenic archaean in the class Methanococci. It was the first archaeon, and third organism, to have its complete genome sequenced. The sequencing identified many genes unique to the archaea. Many of the synthesis pathways for methanogenic cofactors were worked out biochemically in this organism, as were several other archaeal-specific metabolic pathways.
Interspecies hydrogen transfer (IHT) is a form of interspecies electron transfer. It is a syntrophic process by which H2 is transferred from one organism to another, particularly in the rumen and other anaerobic environments.
In enzymology, a formylmethanofuran dehydrogenase (EC 1.2.99.5) is an enzyme that catalyzes the chemical reaction:
