Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source

1982 ◽  
Vol 131 (3) ◽  
pp. 216-223 ◽  
Author(s):  
Margret Bronder ◽  
Hildegard Mell ◽  
Erhard Stupperich ◽  
Achim Kr�ger

1975 ◽  
Vol 152 (3) ◽  
pp. 655-659 ◽  
Author(s):  
B A Haddock ◽  
M W Kendall-Tobias

Measurements were made of energy-dependent quenching of atebrin fluorescence in membrane particles prepared from Escherichia coli grown anaerobically with glycerol as carbon source in the presence of either nitrate or fumarate. It is concluded that this technique can be used to study the functional organization of the anaerobic proton-translocating electron-transport chains that use nitrate or fumarate as terminal electron acceptor.



2017 ◽  
Vol 114 (33) ◽  
pp. E6922-E6931 ◽  
Author(s):  
Maryam Khademian ◽  
James A. Imlay

Microbial cytochrome c peroxidases (Ccp) have been studied for 75 years, but their physiological roles are unclear. Ccps are located in the periplasms of bacteria and the mitochondrial intermembrane spaces of fungi. In this study, Ccp is demonstrated to be a significant degrader of hydrogen peroxide in anoxic Escherichia coli. Intriguingly, ccp transcription requires both the presence of H2O2 and the absence of O2. Experiments show that Ccp lacks enough activity to shield the cytoplasm from exogenous H2O2. However, it receives electrons from the quinone pool, and its flux rate approximates flow to other anaerobic electron acceptors. Indeed, Ccp enabled E. coli to grow on a nonfermentable carbon source when H2O2 was supplied. Salmonella behaved similarly. This role rationalizes ccp repression in oxic environments. We speculate that micromolar H2O2 is created both biologically and abiotically at natural oxic/anoxic interfaces. The OxyR response appears to exploit this H2O2 as a terminal oxidant while simultaneously defending the cell against its toxicity.



1997 ◽  
Vol 36 (6-7) ◽  
pp. 175-182 ◽  
Author(s):  
Thomas Daußmann ◽  
Alexander Aivasidis ◽  
Christian Wandrey

The strictly anaerobic methanogen Methanosarcina barkeri strain Fusaro (DSM 804) was fermented on a 3-liter scale in a CSTR (continuous stirred tank reactor) to obtain almost 10 g biomass dry weight per day. The generation time of the microorganism with methanol as the sole carbon source was 6.0 h, the maximal growth rate 0.115 h−1 correspondingly. In cell-free extracts from the fermented organism active hydrogenases were found. They reduced methyl viologen (MV⊕⊕), an artificial electron acceptor, molecular hydrogen being the substrate. This reaction was used to get electrochemical energy in a biochemical fuel cell. The maximum output of this fuel cell was 2.6 mW. Furthermore, cell-free extracts from M. barkeri showed alcohol dehydrogenase activity under aerobic conditions when N,N′-dimethyl-4-nitrosoaniline (NDMA) was used as an artificial electron acceptor. The NDMA-dependent alcohol dehydrogenase (NDMA-ADH) was purified to homogeneity by column chromatography. It is a homodimeric enzyme consisting of subunits of 45 kDa, the native molecular mass is about 87 kDa. The enzyme is independent of free coenzyme such as NAD, NADP, FMN, FAD and F420, but it possesses a tightly but noncovalently bound NADP(H) cofactor. The purified enzyme exhibited activity only with primary alcohols including aromatic alcohols, but methanol was not accepted. It also catalyzed the stoichiometric dismutation of aldehydes, especially long-chain aldehydes, to form a half mol of each of the corresponding alcohol and acid without addition of an electron carrier. NDMA-ADH from M. barkeri is a novel type of nicotinoprotein in methanogenic bacteria.



1983 ◽  
Vol 135 (1) ◽  
pp. 36-41 ◽  
Author(s):  
Martin Bokranz ◽  
Joachim Katz ◽  
Imke Schr�der ◽  
Anthony M. Roberton ◽  
Achim Kr�ger


Author(s):  
Vivek Kumar Ranjan ◽  
Shriparna Mukherjee ◽  
Subarna Thakur ◽  
Krutika Gupta ◽  
Ranadhir Chakraborty




2013 ◽  
Vol 1 (24) ◽  
pp. 3816 ◽  
Author(s):  
Hao Zhuang ◽  
Qijian Zhang ◽  
Yongxiang Zhu ◽  
Xufeng Xu ◽  
Haifeng Liu ◽  
...  


2008 ◽  
Vol 5 (4) ◽  
pp. 367-374 ◽  
Author(s):  
Jing Wang ◽  
Guiwen Yan ◽  
Mingquan An ◽  
Jieli Liu ◽  
Houming Zhang ◽  
...  


Sign in / Sign up

Export Citation Format

Share Document