The peroxidase activity of cytochrome b6f complex from spinach chloroplasts

Title:

The peroxidase activity of cytochrome b6f complex from spinach chloroplasts

Creator:

Chen, X. B., Hou, C., Li, L. B., and Kuang, T. Y.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:0166c9b4-ef1a-46d7-9153-1920135eaccc
uuid:0166c9b4-ef1a-46d7-9153-1920135eaccc
issn:0300-3604
doi:10.1007/s11099-010-0002-y

Subject:

botanika, botany, cytochrome b6f complex, guaiacol, heme-containing protein, hydrogen peroxide, and peroxidase activity

Type:

model:article and TEXT

Format:

bez média and svazek

Description:

The cytochrome b6f (Cyt b6f) complex, which functions as a plastoquinol-plastocyanin oxidoreductase and mediates the linear electron flow between photosystem II (PSII) and photosystem I (PSI) and the cyclic electron flow around PSI, was isolated from spinach (Spinacia oleracea L.) chloroplasts using n-octyl-β-D-glucopyranoside (β-OG). The preparation was also able to catalyze the peroxidase-like reaction in the presence of hydrogen peroxide (H2O2) and guaiacol. The optimal conditions for peroxidase activity of the preparation included: pH 3.6, ionic strength 0.1, and temperature 35°C. The apparent Michaelis constant (Km) values for H2O2 and guaiacol were 50 mM and 2 mM, respectively. The bimolecular rate constant (k obs) was about 26 M-1 s-1 and the turnover number (K cat) was about 60 min-1 (20 mM guaiacol, 100 mM sodium phosphate, pH 3.6, 25°C, [H2O2]<100mM). These parameters were similar to those of several other heme-containing proteins, such as myoglobin and Cyt c. and X. B. Chen ... [et al.].

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

3-8

Source:

Photosynthetica | 2010 Volume:48 | Number:1

Harvested from:

CDK

Metadata only:

false