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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Limited proteolysis of myoglobin opens channel in ferrochelatase-globin complex for iron to zinc transmetallation

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Author(s):
Paganelli, Marcella O. [1] ; Grossi, Alberto B. [2] ; Dores-Silva, Paulo R. [1] ; Borges, Julio C. [1] ; Cardoso, Daniel R. [1] ; Skibsted, Leif H. [2]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Inst Quim Sao Carlos, Ave Trabalhador Sao Carlense 400, CP 780, BR-13560470 Sao Carlos, SP - Brazil
[2] Univ Copenhagen, Dept Food Sci, Food Chem, Rolighedsvej 30, DK-1958 Frederiksberg C - Denmark
Total Affiliations: 2
Document type: Journal article
Source: Food Chemistry; v. 210, p. 491-499, NOV 1 2016.
Web of Science Citations: 7
Abstract

Recombinant ferrochelatase (BsFECH) from Bacillus subtilis expressed in Escherichia coli BL21(DE3) was found by UV-visible spectroscopy to bind the model substrate tetraphenylporphyrin-sulfonate, TPPS, with K-a = 3.8 10(5) mol/L in aqueous phosphate buffer pH 5.7 at 30 degrees C, and to interact with metmyoglobin with K-a = 1.07 +/- 0.13 10(5) mol/L at 30 degrees C. The iron/zinc exchange in myoglobin occurring during maturation of Parma hams seems to depend on such substrate binding to BsFECH and was facilitated by limited pepsin proteolysis of myoglobin to open a reaction channel for metal exchange still with BsFECH associated to globin. BsFECH increased rate of zinc insertion in TPPS significantly and showed saturation kinetics with an apparent binding constant of Zn(II) to the {[}enzyme-TPPS] complex of 1.3 10(4) mol/L and a first-order rate constant of 6.6 10(-1) s(-1) for dissociation of the tertiary complex, a similar pattern was found for zinc/iron transmetallation in myoglobin. (C) 2016 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 11/51555-7 - Bread and meat for the future
Grantee:Daniel Rodrigues Cardoso
Support Opportunities: Regular Research Grants