Mechanism of dissimilatory sulfite reduction by Desulfovibrio desulfuricans: purification of a membrane-bound sulfite reductase and coupling iwth cytochrome c 3 and hydrogenase

1994 ◽  
Vol 162 (4) ◽  
pp. 255-260
Author(s):  
J. Steuber ◽  
H. Cypionka ◽  
P. M. H. Kroneck
Keyword(s):  
Cytochrome C ◽  
Desulfovibrio Desulfuricans ◽  
Sulfite Reductase ◽  
Membrane Bound

scholarly journals Arrangement of the subunits in solubilized and membrane-bound cytochrome c oxidase from bovine heart.

1975 ◽  
Vol 250 (22) ◽  
pp. 8598-8603 ◽  
Author(s):  
GD Eytan ◽  
RC Carroll ◽  
G Schatz ◽  
E Racker
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Bovine Heart ◽  
Membrane Bound

scholarly journals How Lipids Mobilise Membrane-Bound Cytochrome C Seen by Solid-State NMR

2021 ◽  
Vol 120 (3) ◽  
pp. 284a
Author(s):  
Patrick C.A. van der Wel
Keyword(s):  
Solid State ◽  
Cytochrome C ◽  
Solid State Nmr ◽  
Membrane Bound

scholarly journals Structure of the copper sites in membrane-bound cytochrome c oxidase.

1987 ◽  
Vol 262 (7) ◽  
pp. 3160-3164
Author(s):  
L. Powers ◽  
B. Chance ◽  
Y.C. Ching ◽  
C.P. Lee
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Membrane Bound ◽  
Copper Sites

Cytochrome c, A Membrane-Bound Enzyme

1976 ◽  
pp. 43-86 ◽  
Author(s):  
Jane Vanderkooi ◽  
Maria Erecińska
Keyword(s):  
Cytochrome C ◽  
Membrane Bound

Characterization of the Metamitron Deaminating Enzyme Activity from Sugar Beet ( Beta vulgaris L.) Leaves

1979 ◽  
Vol 34 (11) ◽  
pp. 948-950 ◽  
Author(s):  
Carl Fedtke ◽  
Robert R. Schmidt
Keyword(s):  
Cytochrome C ◽  
Sugar Beet ◽  
Electron Donor ◽  
Nitrogen Atmosphere ◽  
Enzyme Preparations ◽  
Reducing Conditions ◽  
Trade Name ◽  
Membrane Bound

Abstract The enzymatic activity from sugar beet leaves which is responsible for the detoxification of the herbicide metamitron (4-amino-4,5-dihydro-3-methyl-6-phenyl-1, 2, 4-triazin-5-one, trade name Goltix®) has been characterized in vitro. The detoxification occurs by rapid deamination in vivo as well as in vitro. However, the deamination in vitro is only maximal under reducing conditions, i. e. with an electron donor and in a nitrogen atmosphere. The electron donor may be cystein, glutathione, dithionite or ascorbate. The enzymatic deamination further requires the addition of cytochrome c and a “supernatant factor”, which may be replaced by FMN, FAD or DCPIP. However, in the presence of FMN or DCPIP cytochrome c is not essential but only stimulatory. The partic­ulate as well as the soluble metamitron deaminating enzyme preparations obtained take up oxygen when supplied with cysteine and FMN. The particulate enzyme appears in the peroxysome-fraction. It is therefore suggested, that the enzymatic deamination of metamitron in sugar beet leaves is mediated by a proxisomal membrane bound electron transport system which alternatively may reduce oxygen or metamitron (deaminating).

Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. II. Properties of adenosine-5′-phosphosulfate reductase

1970 ◽  
Vol 48 (3) ◽  
pp. 344-354 ◽  
Author(s):  
Ronald M. Lyric ◽  
Isamu Suzuki
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Electron Acceptor ◽  
Desulfovibrio Desulfuricans ◽  
Thiobacillus Denitrificans ◽  
Ph Optimum ◽  
Thiobacillus Thioparus ◽  
Aps Reductase

Adenosine-5′-phosphosulfate (APS) reductase was purified from Thiobacillus thioparus extracts 25- to 46-fold and the properties were studied. The molecular weight was 170 000 and the enzyme had 1 mole of FAD, 8–10 moles of iron, and 4–5 moles of labile sulfide. Cytochrome c as well as ferricyanide served as the electron acceptor. The pH optimum shifted from 7.4 to 9.5 when cytochrome c was used instead of ferricyanide. The Km values for sulfite and AMP were reduced from 2.5 mM and 100 μM to 17 μM and 2.5 μM, respectively, with cytochrome c as electron acceptor. Properties of the T. thioparus enzyme were compared to those of APS reductase isolated from Thiobacillus denitrificans and Desulfovibrio desulfuricans.

scholarly journals Activation of Membrane-associated Procaspase-3 Is Regulated by Bcl-2

1999 ◽  
Vol 144 (5) ◽  
pp. 915-926 ◽  
Author(s):  
Joseph F. Krebs ◽  
Robert C. Armstrong ◽  
Anu Srinivasan ◽  
Teresa Aja ◽  
Angela M. Wong ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Caspase 3 ◽  
Caspase Activity ◽  
Intracellular Membrane ◽  
Caspase Activation ◽  
Intracellular Membranes ◽  
Membrane Bound ◽  
Spontaneous Activation ◽  
Active Caspase

The mechanism by which membrane-bound Bcl-2 inhibits the activation of cytoplasmic procaspases is unknown. Here we characterize an intracellular, membrane-associated form of procaspase-3 whose activation is controlled by Bcl-2. Heavy membranes isolated from control cells contained a spontaneously activatable caspase-3 zymogen. In contrast, in Bcl-2 overexpressing cells, although the caspase-3 zymogen was still associated with heavy membranes, its spontaneous activation was blocked. However, Bcl-2 expression had little effect on the levels of cytoplasmic caspase activity in unstimulated cells. Furthermore, the membrane-associated caspase-3 differed from cytosolic caspase-3 in its responsiveness to activation by exogenous cytochrome c. Our results demonstrate that intracellular membranes can generate active caspase-3 by a Bcl-2–inhibitable mechanism, and that control of caspase activation in membranes is distinct from that observed in the cytoplasm. These data suggest that Bcl-2 may control cytoplasmic events in part by blocking the activation of membrane-associated procaspases.

Sign in / Sign up

Export Citation Format

Share Document