Heme proteins leghemoglobin

Kaur H, Fagerheim I, Grootveld M, Puppo A, Halliwell B (1988) Aromatic hydroxylation of phenylalanine as an assay for hydroxyl radicals application to activated human neutrophils and to the heme protein leghemoglobin. Anal Biochem 172 360-367 Kaur H, Whiteman M, Halliwell B (1997) Peroxynitrite-dependent aromatic hydroxylation and nitration of salicylate and phenylalanine. Is OH radical involved Free Rad Res 26 71-82... 

Kundu, S. Snyder, B. Das. K. Chowdhury, P. Park. J. Petrich. J.W. Hargrove. M.S. The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme. Proteins 2002. 46. 268—277. 

The primary and even tertiary structure of M. and hemoglobins from many different species show striking similarities. M. appears to be phylogenetically the oldest known heme protein, from which hemoglobin evolved as an independent molecule 600 million years ago. M. also appears to be phylogenetically related to Leghemoglobin (see). 

O Brian MR, Kirshbom PM, Maier RJ (1987) Bacterial heme synthesis is required for expression of the leghemoglobin protein but not the apoprotein in soybean root nodules. Proc Natl Acad Sci USA 84 8390-8393... 

Heme derivatives. Name for derivatives of heme, i.e., for iron complexes of the porphyrins and hy-droporphyrins, in the strictest sense of protoporphy-rins. These H. d. are the prosthetic groups of hemo-proteins such as the cytochromes, cytochrome oxidase, peroxidases, catalases, leghemoglobin, nitrite reductases, sulfite reductase see also heme d, heme di, and siroheme. In spite of their similar names heme-rythrin, hemocyanin, hemocuprein, and hemovana-dins do not belong to the H. d. 

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