Lactoperoxidase heme structure characterized by paramagnetic proton NMR spectroscopy

Journal of the American Chemical Society

Volumn 118, Issue 8, 1996, Pages 2103-2104

  Rae, Tracey D ^a   Goff, Harold M ^a  

^a University of Iowa ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEME; LACTOPEROXIDASE;

ARTICLE; ENZYME BINDING; ENZYME STRUCTURE; NUCLEAR MAGNETIC RESONANCE;

EID: 0030000739     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja952650m     Document Type: Article

References (20)

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10. max) and relative intensites in parentheses (given as absorhance of band divided by absorbance of Soret band) are as follows. LPO heme, Soret = 422 nm (1.00) α = 560 nm (0.16). β = 526 nm (0.11): Fe-protoporphyrin IX. Soret = 420 nm (1 00). α = 556 nm (0.22), β = 524 nm (0 13).
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12. 6-DMSO gave a spectrum distinctly different from that displayed in Figure 1 for the heme-peptide species.
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