Results 51 to 60 of about 655,985 (330)

NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants

Communications Biology, 2022
The DsbD protein is normally required for cytochrome c maturation (Ccm) in bacteria. With cytochrome c-rich Shewanella oneidensis as the research model, NapB, the small subunit of the nitrate reductase which is a cytochrome c per se, was found to ...
Kailun Guo, Xue Feng, Weining Sun, Sirui Han, Shihua Wu, Haichun Gao   +5 more
doaj   +1 more source

The complex of cytochrome c and cytochrome c peroxidase: The end of the road?

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2011
Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form a physiological complex in the inter-membrane space of yeast mitochondria, where CcP reduces hydrogen peroxide to water using the electrons provided by ferrous Cc. The Cc-CcP system has been a popular choice of study of interprotein biological electron transfer (ET) and in understanding dynamics ...
Volkov, A.N., Worrall, J.A.R., Nicholls, P.   +2 more
openaire   +4 more sources

Exploring lipid diversity and minimalism to define membrane requirements for synthetic cells

FEBS Letters, EarlyView.
Designing the lipid membrane of synthetic cells is a complex task, in which its various roles (among them solute transport, membrane protein support, and self‐replication) should all be integrated. In this review, we report the latest top‐down and bottom‐up advances and discuss compatibility and complexity issues of current engineering approaches ...
Sergiy Gan, Victoria Scarpelli, Marten Exterkate   +2 more
wiley   +1 more source

Complexation of CcmB with CcmACD safeguards heme translocation for cytochrome c maturation

mLife
Cytochrome c maturation (CCM), a posttranslational modification involving covalent attachment of heme to polypeptides (apocyt c), is essential for the activity and cellular function of cytochromes c.
Yuanyou Xu, Wei Wang, Qianrou Zhang, Sirui Han, Jiahao Wang, Shihua Wu, Haichun Gao   +6 more
doaj   +1 more source

The multidrug and toxin extrusion (MATE) transporter DTX51 antagonizes non‐cell‐autonomous HLS1–AMP1 signaling in a region‐specific manner

FEBS Letters, EarlyView.
The Arabidopsis mutants hls1 hlh1 and amp1 lamp1 exhibit pleiotropic developmental phenotypes. Although the functions of the causative genes remain unclear, they act in the same genetic pathway and are thought to generate non‐cell‐autonomous signals.
Takashi Nobusawa, Makoto Kusaba
wiley   +1 more source

Biochemical mapping reveals a conserved heme transport mechanism via CcmCD in System I bacterial cytochrome c biogenesis

mBio
Heme is a redox-active cofactor for essential processes across all domains of life. Heme’s redox capabilities are responsible for its biological significance but also make it highly cytotoxic, requiring tight intracellular regulation.
Alicia N. Kreiman, Sarah E. Garner, Susan C. Carroll, Molly C. Sutherland   +3 more
doaj   +1 more source

The role of cytochrome c on apoptosis induced by Anagrapha falcifera multiple nuclear polyhedrosis virus in insect Spodoptera litura cells.

PLoS ONE, 2012
There are conflicting reports on the role of cytochrome c during insect apoptosis. Our previous studies have showed that cytochrome c released from the mitochondria was an early event by western blot analysis and caspase-3 activation was closely related ...
Kaiyu Liu, Duanyang Shu, Na Song, Zhongchao Gai, Yuan Yuan, Juan Li, Min Li, Shuying Guo, Jianxin Peng, Huazhu Hong   +9 more
doaj   +1 more source

The role of cytochrome c in caspase activation in Drosophila melanogaster cells [PDF]

, 2002
The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells.
Cakouros, Dimitrios, Dorstyn, Loretta, Hay, Bruce A., Huh, Jun R., Kumar, Sharad, Read, Stuart   +5 more
core   +3 more sources

Revealing the structure of land plant photosystem II: the journey from negative‐stain EM to cryo‐EM

FEBS Letters, EarlyView.
Advances in cryo‐EM have revealed the detailed structure of Photosystem II, a key protein complex driving photosynthesis. This review traces the journey from early low‐resolution images to high‐resolution models, highlighting how these discoveries deepen our understanding of light harvesting and energy conversion in plants.
Roman Kouřil
wiley   +1 more source

The interactions of cytochrome c and porphyrin cytochrome c with cytochrome c oxidase. The resting, reduced and pulsed enzymes [PDF]

European Journal of Biochemistry, 1986
Cytochrome c oxidase forms tight binding complexes with the cytochrome c analog, porphyrin cytochrome c. The behaviour of the reduced and pulsed forms of the oxidase with porphyrin cytochrome c have been followed as functions of ionic strength; this behaviour has been compared with that of the resting oxidase [Kornblatt, Hui Bon Hoa and English (1984 ...
Hue Anh Luu, Jack A. Kornblatt
openaire   +3 more sources