acetylene hydratase

File:Acetylene Hydratase from Pelobacter acetylenicus.png

File:Acetylene Hydratase (PDB code 2E7Z).png

Acetylene hydratase ({{EnzExplorer|4.2.1.112}}, AH) is a bacterial enzyme, originally discovered in the anaerobic microorganism Pelobactor acetylenicus,{{Cite journal| vauthors = Schink B |date=1985|title=Fermentation of acetylene by an obligate anaerobe, Pelobacter acetylenicus sp. nov.| doi = 10.1007/BF00693407|journal=Archives of Microbiology|volume=142 | issue = 3 |pages=295–301|s2cid=9331029 |url=http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-25179 }} that catalyzes the non-redox hydration of acetylene to form acetaldehyde.{{cite journal | vauthors = Kroneck PM | title = Acetylene hydratase: a non-redox enzyme with tungsten and iron-sulfur centers at the active site | journal = Journal of Biological Inorganic Chemistry | volume = 21 | issue = 1 | pages = 29–38 | date = March 2016 | pmid = 26790879 | doi = 10.1007/s00775-015-1330-y | s2cid = 254088239 }}

:C₂H₂ + H₂O → CH₃CHO

The mechanism is thought to involve attachment of acetylene to the metal followed by nucleophilic attack of water. Because acetylene binding to the Mo in nitrogenase lends some support that the mechanism involves a Mo→CH2=CH2 bond. Acetylene inhibits several microbial transformations where it interacts with the active site of the metal-dependent enzymes including hydrogenase and nitrogenase. This enzyme relies on tungsten as the metal center and is the heaviest metal that plays a prominent part in the nitrogen, sulfur and carbon metabolic processes.{{cite journal | vauthors = Liao RZ, Yu JG, Himo F | title = Mechanism of tungsten-dependent acetylene hydratase from quantum chemical calculations | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 52 | pages = 22523–22527 | date = December 2010 | pmid = 21149684 | pmc=3012519 |doi = 10.1073/pnas.1014060108 | doi-access = free }} The [4Fe-4S] cubane keeps the W in the reduced W(IV) state, the most stable reduced oxidation state, while W(VI) is the other stable oxidation state (2nd and 3rd row transition metals are usually most stable in their highest oxidation state). Mo and W enzymes ubiquitously involve W(IV)/W(VI) in the catalysis, however AH is unique since the tungstoenzyme stays as W(IV) in the catalysis.{{cite journal | vauthors = Vidovič C, Belaj F, Mösch-Zanetti NC | title = Soft Scorpionate Hydridotris(2-mercapto-1-methylimidazolyl) borate) Tungsten-Oxido and -Sulfido Complexes as Acetylene Hydratase Models | journal = Chemistry: A European Journal | volume = 26 | issue = 54 | pages = 12431–12444 | date = September 2020 | pmid = 32640122 | doi = 10.1002/chem.202001127|pmc=7589279 }} The tungstoenzyme stays as W(IV) throughout the catalysis because the enzyme catalyzes a non-redox reaction described as the hydration of acetylene to acetaldehyde.{{cite journal | vauthors = Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O | title = Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 9 | pages = 3073–3077 | date = February 2007 | pmid = 17360611 | pmc = 1805521 | doi = 10.1073/pnas.0610407104 | doi-access = free }} The active site tungsten has a distorted octahedral geometry that is coordinated by molybdopterin co-factors along with a cysteine residue coordinated by a water molecule as the sixth ligand. The active site residues are Asp13, Cys12, Trp179, Arg606, Met140 and Ile142. Asp13 plays an important role in assisting the catalysis where the active site residue deprotonates the water hydroxide making it a better nucleophile.