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• W1537489968 endingPage "2587" @default.
• W1537489968 startingPage "2581" @default.
• W1537489968 abstract "A strategic assessment of the contributions of two active-site hydrogen bonds in the binding of nicotinate to recombinant ferric soybean leghaemoglobin a (rLb) was carried out by mutagenic replacement of the hydrogen-bonding residues (H61A and Y30A variants) and by complementary chemical substitution of the carboxylate functionality on the nicotinate ligand. Dissociation constants, Kd (pH 5.5, µ = 0.10 m, 25.0 ± 0.1 °C), for binding of nicotinate to ferric rLb, H61A and Y30A were 1.4 ± 0.3 µm, 19 ± 1 µm and 11 ± 1 µm, respectively; dissociation constants for binding of nicotinamide were, respectively, 38 ± 1 mm, 50 ± 2 mm and 12 ± 1 mm, and for binding of pyridine were 260 ± 50 µm, 4.5 ± 0.5 µm and 66 ± 8 µm, respectively. Binding of cyanide and azide to the H61A and Y30A variants was unaffected by the mutations. The pH-dependence of nicotinate binding for rLb and Y30A was consistent with a single titration process (pKa values 6.9 ± 0.1 and 6.7 ± 0.2, respectively); binding of nicotinate to H61A was independent of pH. Reduction potentials for the rLb and rLb–nicotinate derivatives were 29 ± 2 mV (pH 5.40, 25.0 °C, µ = 0.10 m) and − 65 ± 2 mV (pH 5.42, 25.0 °C, µ = 0.10 m), respectively. The experiments provide a quantitative assessment of the role of individual hydrogen bonds in the binding process, together with a definitive determination of the pKa of His61 and unambiguous evidence that titration of His61 controls binding in the neutral to alkaline region." @default.
• W1537489968 created "2016-06-24" @default.
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• W1537489968 date "2000-05-01" @default.
• W1537489968 modified "2023-10-17" @default.
• W1537489968 title "Investigation of the haem-nicotinate interaction in leghaemoglobin" @default.
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• W1537489968 doi "https://doi.org/10.1046/j.1432-1327.2000.01267.x" @default.
• W1537489968 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10785378" @default.
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