Structural studies of the heme domain of sulfite oxidase: cyanogen bromide fragments

Winge, Dennis R.; Southerland, William M.; Rajagopalan, K.V.; Wiley, Ralph D.

doi:10.1021/bi00603a007

Cited by 5 publications

(2 citation statements)

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“…We cannot of course exclude that deamidation took place at some point during handling of the protein. Table 18 compares positions 48 -67 from chicken sulfite oxidase with the N-terminal sequence of the C-terminal cyanogen bromide fragment from the rat enzyme, as determined by Winge et al [18]. Out of 20 residues, 17 are identical, the other three can be deduced by a single base change in the codon.…”

Section: Discussionmentioning

confidence: 97%

“…Thus the proposed sequence alignment suggests a number of backbone modifications compatible with a generally similar structure : two longer surface Table 18. Partial sequence comparison between chicken sulfite oxidase core and rat sulfite oxidase core The partial sequence of rat sulfite oxidase is taken from [18]. Identical residues are underlined twice; residues that can be deduced by a [22] differs from it in having Gln-13 instead of Glx, GIx-I7 instead of Asn and Asx-19 instead of Gln.…”

Section: Discussionmentioning

confidence: 99%

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Amino Acid Sequence of the 'b5-like' Heme-Binding Domain from Chicken Sulfite Oxidase

Guiard¹,

Lederer²

1979

Eur J Biochem

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We present in this paper the sequence of the heme-binding domain of chicken sulfite oxidase, which can be obtained by chymotryptic digestion of the native enzyme. The results of an automatic degradation have been reported previously. In the present work peptides were obtained from the heme-binding domain by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 protease ; they were manually sequenced by the dansyl/Edman procedure. The evidence thus obtained is sufficient to completely establish the order of the 97 residues. In addition, two rounds of Edman degradation on sulfite oxidase itself allowed us to identify the same two residues, H-Ala-Pro, present at the N-terminus of the heme-binding domain; this result suggests that the latter constitutes the amino-terminal end of the sulfite oxidase peptide chain.The data presented here confirm the strong similarity between sulfite oxidase and microsomal cytochrome b5 already suggested by our first results. A sequence alignment is proposed for the two proteins. Inspection of the calf liver cytochrome b5 three-dimensional model together with the alignment suggests a similar overall structure for sulfite oxidase core with a limited number of backbone modifications. Our results point to a common evolutionary origin for sulfite oxidase core and microsomal cytochrome b5.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%