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Stanniocalcin 1 binds hemin through a partially conserved heme regulatory motif.

Abstract：

:Hemin (iron protoporphyrin IX) is a necessary component of many proteins, functioning either as a cofactor or an intracellular messenger. Hemoproteins have diverse functions, such as transportation of gases, gas detection, chemical catalysis and electron transfer. Stanniocalcin 1 (STC1) is a protein involved in respiratory responses of the cell but whose mechanism of action is still undetermined. We examined the ability of STC1 to bind hemin in both its reduced and oxidized states and located Cys(114) as the axial ligand of the central iron atom of hemin. The amino acid sequence differs from the established (Cys-Pro) heme regulatory motif (HRM) and therefore presents a novel heme binding motif (Cys-Ser). A STC1 peptide containing the heme binding sequence was able to inhibit both spontaneous and H(2)O(2) induced decay of hemin. Binding of hemin does not affect the mitochondrial localization of STC1.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Westberg JA,Jiang J,Andersson LC

doi

10.1016/j.bbrc.2011.05.002

subject

Has Abstract

pub_date

2011-06-03 00:00:00

pages

266-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)00748-0

journal_volume

409

pub_type

杂志文章

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