Journal
SCIENCE
Volume 344, Issue 6179, Pages 75-78Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1250808
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Funding
- Natural Sciences and Engineering Research Council of Canada
- Academy of Finland
- Canada Research Chairs Program
- Canadian Foundation for Innovation
- Nova Scotia Research and Innovation Trust Fund
- Technology Industries of Finland Centennial Foundation
- University of Jyvaskyla
- GreenCentre Canada
- Encana Corporation
- Magnus Ehrnrooth Foundation
- Springboard
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Why does cyanide not react destructively with the proximal iron center at the active site of 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase, an enzyme central to the biosynthesis of ethylene in plants? It has long been postulated that the cyanoformate anion, [NCCO2](-), forms and then decomposes to carbon dioxide and cyanide during this process. We have now isolated and crystallographically characterized this elusive anion as its tetraphenylphosphonium salt. Theoretical calculations show that cyanoformate has a very weak C-C bond and that it is thermodynamically stable only in low dielectric media. Solution stability studies have substantiated the latter result. We propose that cyanoformate shuttles the potentially toxic cyanide away from the low dielectric active site of ACC oxidase before breaking down in the higher dielectric medium of the cell.
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