Anesthesia of Protoplasm

Kelly, F H

doi:10.1097/00000542-194501000-00042

Anesthesiology

1945

DOI: 10.1097/00000542-194501000-00042

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Anesthesia of Protoplasm

F H Kelly¹

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1982

1983

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“…Like N2 fixation, the reaction required Mg ATP and a reductant and was inhibited by carbon monoxide. CH3NC reduction was later shown to be a general property of N2-fixing organisms [e.g., Hardy & Jackson (1967), Kelly (1968) , Munson & Burris (1969), and Biggins & Postgate (1969) ]. Kelly et al (1967) examined CH3NC reduction in D20 and demonstrated that all methane appeared as CD4 and thus arose from the isocyanide carbon.…”

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confidence: 99%

“…Both effects occur in the same relative order, implying productive (substrate) and nonproductive (inhibitor) modes of binding of CH3NC to the same site. ethylene and ethane, are formed (Kelly et al, 1967;Hardy & Jackson, 1967; Kelly, 1968). Using D20, Kelly (1968) demonstrated that both carbon atoms in the C2 products arose from the isocyanide carbon.…”

mentioning

confidence: 99%

“…Using D20, Kelly (1968) demonstrated that both carbon atoms in the C2 products arose from the isocyanide carbon. Although it was originally suggested that the C2 products were formed by reaction of two enzyme-bound C, radicals (Kelly et al, 1967), further experimentation (Kelly, 1968;Hardy & Jackson, 1967) and kinetic analysis (Hardy, 1979) showed that C2 product formation was dependent upon both CH4 formation and the free CH3NC concentration. On the basis of this information, Hardy (1979) suggested a reduction followed by an insertion mechanism whereby C2 products are formed by interaction of a single bound Ct radical with a free molecule of CH3NC.…”

mentioning

confidence: 99%

“…Observations of CO stimulation of C2 product formation were later interpreted (Hardy, 1979) as an indication that CO might be inserted to form C2 products. The C3 products propylene and propane were also formed during CH3NC reduction (Kelly, 1968; Hardy, 1979), albeit in very small amounts.…”

mentioning

confidence: 99%

“…Methyl isocyanide concentration dependence experiments were complicated by the observation that the rate of methane formation began to decrease above 5 mM CH3NC (Kelly, 1968;Hwang & Burris, 1972). Total electron flow was not measured so it was not clear if the decrease in methane formation was being offset by an increase in hydrogen evolution or if total electron flow was being inhibited (Hwang & Burris, 1972).…”

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Nitrogenase reactivity: methyl isocyanide as substrate and inhibitor

Rubinson¹,

Corbin²,

Burgess³

1983

Biochemistry

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We have examined the interaction of methyl isocyanide with the purified component proteins of Azotobacter vinelandii nitrogenase (Av1 and Av2). CH3NC was shown to be a potent reversible inhibitor (Ki = 158 microM) of total electron flow, apparently uncoupling magnesium adenosine 5'-triphosphate hydrolysis from electron transfer to substrate. CH3NC is a substrate (Km = 0.688 mM at Av2/Av1 = 8), and extrapolation of the data indicates that at high enough CH3NC concentration, H2 evolution can be eliminated. The products are methane plus methylamine (six electrons) and dimethylamine (four electrons). There is an excess (relative to methane) of methylamine formed, which may arise by hydrolysis of a two-electron intermediate. A rapid high-performance liquid chromatography/fluorescence method was developed for methylamine determination. The products C2H4 and C2H6 appear to be formed via a reduction followed by an insertion mechanism. CH3NC appears to be reduced at an enzyme state more oxidized than the one responsible for H2 evolution or N2 reduction. Other substrates (C2H2 greater than N2 congruent to azide greater than N2O) all both relieve CH3NC inhibition and inhibit CH3NC reduction. Both effects occur in the same relative order, implying productive (substrate) and nonproductive (inhibitor) modes of binding of CH3NC to the same site.

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confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Nitrogenase reactivity: methyl isocyanide as substrate and inhibitor

Rubinson¹,

Corbin²,

Burgess³

1983

Biochemistry

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Nitrogenase reactivity: cyanide as substrate and inhibitor

Li¹,

Burgess²,

Corbin³

1982

Biochemistry

109

150

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We have examined the reduction of cyanide by using the purified component proteins of nitrogenase (Av1 and Av2). The previously reported self-inhibition phenomenon was found to be an artifact. One of the two species present in cyanide solutions, CN-, was shown to be a potent reversible inhibitor (Ki = 27 microM) of total electron flow, apparently uncoupling MgATP hydrolysis and electron transfer. There appears to be no differential effect of CN- on the specific activities of Av1 and Av2 nor is there any apparent irreversible physical damage to Av2. CN- inhibition is completely reversed by low levels of CO, implying a common binding site. Azide partially relieves the inhibitory effect, but other substrates and inhibitors (N2, C2H2, N2O, H2) have no effect. The other species present in cyanide solutions, HCN, was shown to be the substrate (Km = 4.5 mM at Av2/Av1 = 8), and extrapolation of the data indicates that at high enough HCN concentration H2 evolution can be eliminated. The products are methane plus ammonia (six electrons), and methylamine (four electrons). There is an excess (relative to methane) of ammonia formed, which, according to electron balance studies, may arise from a two-electron intermediate. Both nitrous oxide and acetylene (but not N2) influence the distribution of cyanide reduction products, implying simultaneous binding. HCN appears to bind to and be reduced at an enzyme state more oxidized than the one responsible for either H2 evolution or N2 reduction.

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Anesthesia of Protoplasm

Cited by 2 publications

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Nitrogenase reactivity: methyl isocyanide as substrate and inhibitor

Nitrogenase reactivity: methyl isocyanide as substrate and inhibitor

Nitrogenase reactivity: cyanide as substrate and inhibitor

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