負の協同性

WordNet

reckoned in a direction opposite to that regarded as positive; "negative interest rates"
a piece of photographic film showing an image with light and shade or colors reversed
a reply of denial; "he answered in the negative"
not indicating the presence of microorganisms or disease or a specific condition; "the HIV test was negative" (同)disconfirming
having a negative charge; "electrons are negative" (同)electronegative, negatively charged
characterized by or displaying negation or denial or opposition or resistance; having no positive features; "a negative outlook on life"; "a colorless negative personality"; "a negative evaluation"; "a negative reaction to an advertising campaign"
expressing or consisting of a negation or refusal or denial
having the quality of something harmful or unpleasant; "ran a negative campaign"; "delinquents retarded by their negative outlook on life"
less than zero; "a negative number"

PrepTutorEJDIC

『否定の』,反対の / 『消極的な』,控えめの / 陰電気の;(数値が)負の,マイナスの(minus);(写真が)陰画の,ネガの;(医学検査結果が)陰性の / 『否定』,拒否,「いやだ」と言うこと / 否定語[句] / 《the~》(特に討論会の)反対者側,反対派 / (電気分解に用いる)陰極板 / (数値の)負数 / (写真の)陰画,ネガ / 《しばしば受動態に用いて》…‘に'反対投票をする / =negate

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1. グラム陰性桿菌性髄膜炎の疫学および臨床的特徴 epidemiology and clinical features of gram negative bacillary meningitis
2. インスリン受容体の構造および機能 structure and function of the insulin receptor
3. グラム陰性桿菌性髄膜炎の診断および治療 diagnosis and treatment of gram negative bacillary meningitis
4. 診断的検査の評価 evaluating diagnostic tests
5. 神経筋疾患および胸壁疾患における夜間の非侵襲的換気補助の種類 types of noninvasive nocturnal ventilatory support in neuromuscular and chest wall disease

English Journal

The O(2) reduction and proton pumping gate mechanism of bovine heart cytochrome c oxidase.

Yoshikawa S, Muramoto K, Shinzawa-Itoh K.AbstractX-ray structures of bovine heart cytochrome c oxidase with bound respiratory inhibitors (O(2) analogues) have been determined at 1.8-2.05A resolution to investigate the function of the O(2) reduction site which includes two metal sites (Fe(a3)(2+) and Cu(B)(1+)). The X-ray structures of the CO- and NO-bound derivatives indicate that although there are three possible electron donors that can provide electrons to the bound O(2), located in the O(2) reduction site, the formation of the peroxide intermediate is effectively prevented to provide an O(2)-bound form as the initial intermediate. The structural change induced upon binding of CN(-) suggests a non-sequential 3-electoron reduction of the bound O(2)(-) for the complete reduction without release of any reactive oxygen species. The X-ray structure of the derivative with CO bound to Cu(B)(1+) after photolysis from Fe(a3)(2+) demonstrates weak side-on binding. This suggests that Cu(B) controls the O(2) supply to Fe(a3)(2+) without electron transfer to provide sufficient time for collection of protons from the negative side of the mitochondrial membrane. The proton-pumping pathway of bovine heart cytochrome c oxidase includes a hydrogen-bond network and a water channel located in tandem between the positive and negative side of the mitochondrial membrane. Binding of a strong ligand to Fe(a3) induces a conformational change which significantly narrows the water channel and effectively blocks the back-leakage of protons from the hydrogen bond network. The proton pumping mechanism proposed by these X-ray structural analyses has been functionally confirmed by mutagenesis analyses of bovine heart cytochrome c oxidase. This article is part of a Special Issue entitled: Allosteric cooperativity in respiratory proteins.
Biochimica et biophysica acta.Biochim Biophys Acta.2011 Oct;1807(10):1279-86. Epub 2011 Jun 21.
X-ray structures of bovine heart cytochrome c oxidase with bound respiratory inhibitors (O(2) analogues) have been determined at 1.8-2.05A resolution to investigate the function of the O(2) reduction site which includes two metal sites (Fe(a3)(2+) and Cu(B)(1+)). The X-ray structures of the CO- and
PMID 21718684

Kinetic and Chemical Mechanisms of Homocitrate Synthase from Thermus thermophilus.

Kumar VP, West AH, Cook PF.SourceFrom the Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019.
The Journal of biological chemistry.J Biol Chem.2011 Aug 19;286(33):29428-39. Epub 2011 Jul 6.
The homocitrate synthase from Thermus thermophilus (TtHCS) is a metal-activated enzyme with either Mg(2+) or Mn(2+) capable of serving as the divalent cation. The enzyme exhibits a sequential kinetic mechanism. The mechanism is steady state ordered with α-ketoglutarate (α-Kg) binding prior to acet
PMID 21733842

Japanese Journal

Positive and negative cooperativity of modularly assembled zinc fingers.

Imanishi Miki,Nakamura Atsushi,Morisaki Tatsuya,Futaki Shiroh
Biochemical and biophysical research communications 387(3), 440-443, 2009-09-25
… Our results indicate that not only a positive cooperativity but also a context-dependent reduction in the DNA binding activity can be induced by assembling zinc finger modules. …
NAID 120002753564