Abstract:
:A kinetic study of CO(2) hydration was carried out using the water-soluble zinc model complex with water-soluble nitrilotris(2-benzimidazolylmethyl-6-sulfonate) L1S, [L1SZn(OH(2))](-), mimicking the active site of carbonic anhydrase, in the presence and absence of anion inhibitors NCS(-) and Cl(-). The obtained rate constants k(cat) for CO(2) hydration were 5.9x10(2), 1. 7x10(3), and 3.1x10(3) M(-1) s(-1) at 5, 10, and 15 degrees C, respectively: the k(cat)=ca. 10(4) M(-1) s(-1) extrapolated towards 25 degrees C has been the largest among the reported k(cat) using zinc model complexes for carbonic anhydrase. It was also revealed that NCS(-), Cl(-) and acetazolamide play a role of inhibitors by the decrease of k(cat): 7x10(2) and 2x10(3) M(-1) s(-1) for NCS(-) and Cl(-) at 15 degrees C, respectively. The sequence of their magnitudes in k(cat) is Cl(-) approximately acetazolamide>NCS(-), where the sequence Cl(-)>NCS(-) is confirmed for native carbonic anhydrase. The difference of k(cat) or k(obs) between NCS(-) and Cl(-) resulted from that between the stability constants K(st)=2x10(3) for [L1SZn(NCS)](2-) and 1x10(2) M(-1) for [L1SZnCl](2-) in D(2)O: for water-insoluble tris(2-benzimidazolylmethyl)amine L1, K(st)=1.8x10(4) for [L1Zn(NCS)](2-) and 1.5x10(3) M(-1) for [L1ZnCl](2-)in CD(3)CN/D(2)O (50% v/v). The crystal structure of anion-binding zinc model complexes [L1Zn(OH(2))](0.5)[L1ZnCl](0.5) (ClO(4))(1.5) 1(0.5)2(0.5)(ClO(4))(1.5) was revealed by X-ray crystallography. The geometry around Zn(2+) in 1 and 2 was tetrahedrally coordinated by three benzimidazolyl nitrogen atoms and one oxygen atom of H(2)O, or Cl(-).
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Nakata K,Shimomura N,Shiina N,Izumi M,Ichikawa K,Shiro Mdoi
10.1016/s0162-0134(01)00419-6subject
Has Abstractpub_date
2002-04-28 00:00:00pages
255-66issue
3-4eissn
0162-0134issn
1873-3344pii
S0162013401004196journal_volume
89pub_type
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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abstract::With its about 100,000 three-dimensional structures, the Protein Data Bank is a copious source of information: it contains also some hundreds of structures of macromolecules complexed with lanthanide cations, which are examined here. These cations, which are found in a wide variety of protein types, were introduced to...
journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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abstract::Deposition of beta sheets of islet amyloid polypeptide (IAPP) in pancreatic tissue is implicated in the aetiology of type 2 diabetes mellitus (T2DM). IAPP is cleaved from its precursor protein, pro-islet amyloid polypeptide (ProIAPP) and incomplete cleavage results in ProIAPP(1-48), which is found co-deposited with IA...
journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
doi:10.1016/s0162-0134(96)00122-5
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pub_type: 杂志文章,评审
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
doi:10.1016/0162-0134(89)80011-x
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pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
pub_type: 杂志文章
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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