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15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate.
Biochemistry. 1990 Sep 11;29(36):8345-50. doi: 10.1021/bi00488a021.
Biochemistry. 1990.
PMID: 2252894
13C NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase.
Rajagopalan JS, Taylor KM, Jaffe EK.
Rajagopalan JS, et al.
Biochemistry. 1993 Apr 20;32(15):3965-72. doi: 10.1021/bi00066a017.
Biochemistry. 1993.
PMID: 8471608
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31P NMR spectroscopic studies on purified, native and cloned, expressed forms of NADPH-cytochrome P450 reductase.
Narayanasami R, Otvos JD, Kasper CB, Shen A, Rajagopalan J, McCabe TJ, Okita JR, Hanahan DJ, Masters BS.
Narayanasami R, et al.
Biochemistry. 1992 May 5;31(17):4210-8. doi: 10.1021/bi00132a009.
Biochemistry. 1992.
PMID: 1567869
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