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方案
97%
表单
liquid
折射率
n20/D 1.396 (lit.)
密度
0.795 g/mL at 25 °C (lit.)
官能团
amine
isonitrile
储存温度
2-8°C
SMILES字符串
CCCC[N+]#[C-]
InChI
1S/C5H9N/c1-3-4-5-6-2/h3-5H2,1H3
InChI key
FSBLVBBRXSCOKU-UHFFFAOYSA-N
应用
用异氰酸丁酯研究了从 生氢一氧化碳嗜热菌中分离得到的一氧化碳脱氢酶-II的晶体结构 。本研究的目的是探讨 NO 激活血蛋白可溶性鸟苷酸环化酶的机制 。
生化/生理作用
丁基异腈与细胞色素 P450 中血红素的三价铁和二价铁形成络合物 。
其他说明
可能形成浑浊和/或沉淀，对纯度无影响。
警示用语：
Danger
危险分类
Acute Tox. 4 Oral - Flam. Liq. 2
储存分类代码
3 - Flammable liquids
WGK
WGK 3
闪点(°F)
69.8 °F - closed cup
闪点(°C)
21 °C - closed cup
个人防护装备
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
其他客户在看
Y Imai et al.
Biochimica et biophysica acta, 1337(1), 66-74 (1997-01-04)
Heme-external ligand interactions of P-450nor were examined spectrophotometrically and compared with those of other P-450s. Most nitrogenous ligands induced type II spectral changes on binding to ferric P-450nor, as did other P-450s. In contrast with other P-450s, 2-methylpyridine and 1-butanol
Akira Ikezaki et al.
Chemical communications (Cambridge, England), (19)(19), 2257-2259 (2008-05-09)
Addition of tert-butylisocyanide (tBuNC) to a CD2Cl2 solution of the bis(perchlorato)(meso-tetramesitylporphyrinato) iron(III) cation radical leads to the formation of the corresponding bis(adduct), [Fe(TMP)(tBuNC)2]2+, whose electronic structure is in sharp contrast to that of the corresponding imidazole(HIm) complex, [Fe(TMP)(HIm)2]2+; the former
T H Tahirov et al.
Nature structural biology, 3(5), 459-464 (1996-05-01)
We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of
C Mouro et al.
European journal of biochemistry, 267(1), 216-221 (1999-12-22)
An 1H-NMR study of ferric cytochrome P450cam in different paramagnetic states was performed. Assignment of three heme methyl resonances of the isocyanide adduct of cytochrome P450 in the ferric low-spin state was recently performed using electron exchange in the presence
D Barrick et al.
Biochemistry, 40(13), 3780-3795 (2001-04-13)
The linkage between the proximal histidines and the proximal polypeptide in normal adult human hemoglobin (Hb A) has been proposed to play a major role in transmitting allosteric effects between oxygen binding sites [Perutz, M. F. (1970) Nature 228, 726-734].
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