WordNet

(biochemistry) a class of hemoprotein whose principal biological function is electron transfer (especially in cellular respiration)
the 6th letter of the Roman alphabet (同)f

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feedの過去・過去分詞
連邦政府役人
farad / forte

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/02/14 15:49:16」(JST)

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Cytochrome f is the largest subunit of cytochrome b₆f complex (plastoquinol—plastocyanin reductase; EC 1.10.99.1). In its structure and functions, the cytochrome b6f complex bears extensive analogy to the cytochrome bc1 complex of mitochondria and photosynthetic purple bacteria. Cytochrome f (cyt f) plays a role analogous to that of cytochrome c1, in spite of their different structures.^[1]

The 3D structure of Brassica rapa (Turnip) cyt f has been determined.^[2] The lumen-side segment of cyt f includes two structural domains: a small one above a larger one that, in turn, is on top of the attachment to the membrane domain. The large domain consists of an anti-parallel beta-sandwich and a short haem-binding peptide, which form a three-layer structure. The small domain is inserted between beta-strands F and G of the large domain and is an all-beta domain. The haem nestles between two short helices at the N terminus of cyt f. Within the second helix is the sequence motif for the c-type cytochromes, CxxCH (residues 21-25), which is covalently attached to the haem through thioether bonds to Cys-21 and Cys-24. His-25 is the fifth haem iron ligand. The sixth haem iron ligand is the alpha-amino group of Tyr-1 in the first helix.^[2] Cyt f has an internal network of water molecules that may function as a proton wire.^[2] The water chain appears to be a conserved feature of cyt f.

References

^ Prince RC, George GN (June 1995). "Cytochrome f revealed". Trends Biochem. Sci. 20 (6): 217–8. doi:10.1016/S0968-0004(00)89018-0. PMID 7631417.
^ ^a ^b ^c Martinez SE, Huang D, Ponomarev M, Cramer WA, Smith JL (June 1996). "The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain". Protein Sci. 5 (6): 1081–92. doi:10.1002/pro.5560050610. PMC 2143431. PMID 8762139.

External links

Cytochrome f at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the public domain Pfam and InterPro IPR002325

UpToDate Contents

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English Journal

Photoprotection Conferred by Changes in Photosynthetic Protein Levels and Organization during Dehydration of a Homoiochlorophyllous Resurrection Plant.

Charuvi D1, Nevo R1, Shimoni E1, Naveh L1, Zia A1, Adam Z1, Farrant JM1, Kirchhoff H1, Reich Z2.
Plant physiology.Plant Physiol.2015 Apr;167(4):1554-65. doi: 10.1104/pp.114.255794. Epub 2015 Feb 23.
During desiccation, homoiochlorophyllous resurrection plants retain most of their photosynthetic apparatus, allowing them to resume photosynthetic activity quickly upon water availability. These plants rely on various mechanisms to prevent the formation of reactive oxygen species and/or protect thei
PMID 25713340

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane.

Zoschke R1, Barkan A2.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Mar 31;112(13):E1678-87. doi: 10.1073/pnas.1424655112. Epub 2015 Mar 16.
Chloroplast genomes encode ∼37 proteins that integrate into the thylakoid membrane. The mechanisms that target these proteins to the membrane are largely unexplored. We used ribosome profiling to provide a comprehensive, high-resolution map of ribosome positions on chloroplast mRNAs in separated m
PMID 25775549

Tomato fruit chromoplasts behave as respiratory bioenergetic organelles during ripening.

Renato M1, Pateraki I1, Boronat A2, Azcón-Bieto J2.
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During tomato (Solanum lycopersicum) fruit ripening, chloroplasts differentiate into photosynthetically inactive chromoplasts. It was recently reported that tomato chromoplasts can synthesize ATP through a respiratory process called chromorespiration. Here we show that chromoplast oxygen consumption
PMID 25125503

Japanese Journal

固液界面におけるチトクロームcの固定化と直接電子移動反応に対する表面修飾の効果 (有機エレクトロニクス)

電子情報通信学会技術研究報告 = IEICE technical report : 信学技報 116(2), 1-5, 2016-04-08
NAID 40020818955

固液界面におけるチトクロームcの固定化と直接電子移動反応に対する表面修飾の効果 (シリコン材料・デバイス)

電子情報通信学会技術研究報告 = IEICE technical report : 信学技報 116(1), 1-5, 2016-04-08
NAID 40020818439

C-13-1 スラブ光導波路分光法を用いたガラス/溶液界面からのチトクロームcの脱離反応のその場観察(C-13.有機エレクトロニクス,一般セッション)

電子情報通信学会総合大会講演論文集 2016年_エレクトロニクス(2), 114, 2016-03-01
NAID 110010026196

Related Pictures

★リンクテーブル★

リンク元	「シトクロムf」「チトクロムf」
関連記事	「F」「fd」

「シトクロムf」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Apocytochr_F_C
	cytochrome f from the b6f complex of Phormidium laminosum
Identifiers
Symbol	Apocytochr_F_C
Pfam	PF01333
Pfam clan	CL0105
InterPro	IPR002325
PROSITE	PDOC00169
SCOP	1ctm
SUPERFAMILY	1ctm
TCDB	3.D.3
OPM superfamily	345
OPM protein	3h1j
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary