Revisiting the Mechanism of the Anaerobic Coproporphyrinogen III Oxidase HemN

2019 ◽  
Vol 58 (19) ◽  
pp. 6235-6238 ◽  
Author(s):  
Xinjian Ji ◽  
Tianlu Mo ◽  
Wan‐Qiu Liu ◽  
Wei Ding ◽  
Zixin Deng ◽  
...  
Keyword(s):  
Coproporphyrinogen Iii Oxidase

scholarly journals Analysis of hemF Gene Function and Expression in Rhodobacter sphaeroides 2.4.1

2006 ◽  
Vol 188 (2) ◽  
pp. 801-804 ◽  
Author(s):  
Jill H. Zeilstra-Ryalls ◽  
Kathryn L. Schornberg
Keyword(s):  
Mutant Strain ◽  
Rhodobacter Sphaeroides ◽  
Gene Function ◽  
Regulatory Protein ◽  
Aerobic Conditions ◽  
Coproporphyrinogen Iii Oxidase

ABSTRACT The hemF gene of Rhodobacter sphaeroides 2.4.1 is predicted to code for an oxygen-dependent coproporphyrinogen III oxidase. We found that a HemF− mutant strain is unable to grow under aerobic conditions. We also determined that hemF expression is controlled by oxygen, which is mediated, at least in part, by the response regulatory protein PrrA.

scholarly journals Anaerobic and aerobic coproporphyrinogen III oxidases of Rhodopseudomonas spheroides. Mechanism and stereochemistry of vinyl group formation

1983 ◽  
Vol 209 (3) ◽  
pp. 709-718 ◽  
Author(s):  
J S Seehra ◽  
P M Jordan ◽  
M Akhtar
Keyword(s):  
Hydrogen Atom ◽  
Group Formation ◽  
Side Chains ◽  
Improved Method ◽  
Conversion Formula ◽  
Coproporphyrinogen Iii Oxidase ◽  
Rhodopseudomonas Spheroides ◽  
Vinyl Group

An improved method for the preparation of various species of porphobilinogen stereospecifically labelled with 3H in the side chains (at C-6, C-7 and C-8) is described. These labelled samples were used to study the mechanism and stereochemistry of anaerobic as well as aerobic coproporphyrinogen III oxidase of light-grown Rhodopseudomonas spheroides. It was shown that both the oxidases catalyse the conversion of the propionate side chains of coproporphyrinogen III into the vinyl groups of protoporphyrinogen IX, (formula; see text) with the labilization of the pro-S-hydrogen atom at the beta-position. These results are similar to those previously recorded for such conversions in animal and plant systems. In the light of the cumulative information available to date, mechanisms for the conversion, (formula; see text) are discussed and doubt is cast on the participation of hydroxylated intermediates in the process.

scholarly journals The Substrate Radical of Escherichia coli Oxygen-independent Coproporphyrinogen III Oxidase HemN

2006 ◽  
Vol 281 (23) ◽  
pp. 15727-15734 ◽  
Author(s):  
Gunhild Layer ◽  
Antonio J. Pierik ◽  
Matthias Trost ◽  
Steve E. Rigby ◽  
Helen K. Leech ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Coproporphyrinogen Iii Oxidase

scholarly journals Oxygen-independent Coproporphyrinogen-III Oxidase HemN fromEscherichia coli

2002 ◽  
Vol 277 (37) ◽  
pp. 34136-34142 ◽  
Author(s):  
Gunhild Layer ◽  
Knut Verfürth ◽  
Esther Mahlitz ◽  
Dieter Jahn
Keyword(s):  
Fromescherichia Coli ◽  
Coproporphyrinogen Iii Oxidase

scholarly journals Role of Mitochondria in Regulating Lutein and Chlorophyll Biosynthesis in Chlorella pyrenoidosa under Heterotrophic Conditions

Marine Drugs ◽  
2018 ◽  
Vol 16 (10) ◽  
pp. 354 ◽  
Author(s):  
Zhi-hui Liu ◽  
Tao Li ◽  
Qing-yu He ◽  
Zheng Sun ◽  
Yue Jiang
Keyword(s):  
Phosphoenolpyruvate Carboxykinase ◽  
Chlorophyll Biosynthesis ◽  
Photosynthetic Pigment ◽  
Chlorella Pyrenoidosa ◽  
Transport Chain ◽  
Genes Encoding ◽  
Green Alga Chlorella ◽  
Pigment Biosynthesis ◽  
Coproporphyrinogen Iii Oxidase ◽  
Protein Alterations

The green alga Chlorella pyrenoidosa can accumulate lutein and chlorophyll under heterotrophic conditions. We propose that the mitochondrial respiratory electron transport chain (mRET) may be involved in this process. To verify this hypothesis, algal cells were treated with different mRET inhibitors. The biosynthesis of lutein and chlorophyll was found to be significantly stimulated by salicylhydroxamic acid (SHAM), whereas their contents substantially decreased after treatment with antimycin A and sodium azide (NaN3). Proteomic studies revealed profound protein alterations related to the redox and energy states, and a network was proposed: The up-regulation of peroxiredoxin reduces oxidized glutathione (GSSG) to reduced glutathione (GSH); phosphoenolpyruvate carboxykinase (PEPCK) catalyzes the conversion of oxaloacetic acid to phosphoenolpyruvate, and after entering the methylerythritol phosphate (MEP) pathway, 4-hydroxy-3-methylbut-2-en-1yl diphosphate synthase reduces 2-C-methyl-d-erythritol-2,4-cyclodiphosphate (ME-Cpp) to 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP), which is closely related to the synthesis of lutein; and coproporphyrinogen III oxidase and ChlI play important roles in the chlorophyll biosynthetic pathway. These results supported that for the heterotrophic C. pyrenoidosa, the signaling, oriented from mRET, may regulate the nuclear genes encoding the enzymes involved in photosynthetic pigment biosynthesis.

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