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- W2089078037 abstract "Modification of ribulose bisphosphate carboxylase with tetranitromethane C(NO2)4 resulted in a total loss of enzyme activity. The fully activated enzyme was more kinetically sensitive to modification by tetranitromethane than the non-activated enzyme. Modification by C(NO2)4 was not observed at pH 6.0 and was more pronounced in the pH range of 8–9. Several lines of evidence indicate that oxidation of thiol groups are not involved in the modification of the enzyme by tetranitromethane. Ribulose bisphosphate offered complete protection against tetranitromethane inactivation with a K 12 (protection) of 280 μM. Some of the affectors of the enzyme gave substantial protection against tetranitromethane modification. Spectrophotometric measurements of nitrotyrosine indicated that modification results from the nitration of one tyrosine residue per 70 000 dalton combination of large and small subunit. No structural changes were observed in the tetranitromethane modified enzyme within the range of concentrations of tetranitromethane used. From the experimental results it was strongly suggested that ribulose bisphosphate carboxylase has an essential tyrosine residue at or near the active site." @default.
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- W2089078037 date "1982-11-01" @default.
- W2089078037 modified "2023-09-27" @default.
- W2089078037 title "Modification of essential tyrosine residues of spinach ribulose 1,5-bisphosphate carboxylase" @default.
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- W2089078037 doi "https://doi.org/10.1016/0304-4211(82)90137-7" @default.
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