Abstract：
:The interaction between cadmium and yeast hexokinase was studied. Cadmium produces changes in the aggregation state of the protein and large structures with a large molecular mass were formed. This phenomenon occurs without large modifications to the secondary structure. During this change the enzyme maintains a high level of activity in the monomer as well as in aggregate form. This implies that the enzyme function is not greatly affected by the change and it maintains its active sites without significant modifications. According to kinetic measurements with both glucose and ATP as a variable substrate, cadmium causes a mixed-type inhibition with a main uncompetitive component. Binding experiments show that the protein presents negative cooperative binding with cadmium at various temperatures (298, 303 and 313 K) and a progressive loss in metal union with concentration depending on the temperature. The total union percentage decreases as the metal concentration increases. This is probably due to the aggregation process, which affects the binding sites for the metal and also for the substrate. Labile interactions are more persistent than specific interactions in accordance with the solvation parameter.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Olmo R,Blanco MD,Teijón C,Miguel del Socorro J,Teijón JMdoi
10.1016/s0162-0134(01)00367-1subject
Has Abstractpub_date
2002-04-10 00:00:00pages
107-14issue
1-2eissn
0162-0134issn
1873-3344pii
S0162013401003671journal_volume
89pub_type
杂志文章abstract：:The binding of acetazolamide, p-fluorobenzensulfonamide, p-toluenesulfonamide, and sulfanilamide to nickel(II)-substituted carbonic anhydrase II has been studied by 1H NMR and electronic absorption spectroscopies. These inhibitors bind to the metal ion forming 1:1 complexes and their affinity constants were determined...
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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
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/j.jinorgbio.2012.02.020
更新日期：2012-06-01 00:00:00
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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,评审
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更新日期：2014-04-01 00:00:00
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journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
doi：10.1016/j.jinorgbio.2004.07.011
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journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
doi：10.1016/j.jinorgbio.2013.09.008
更新日期：2013-12-01 00:00:00
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journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
doi：10.1016/0162-0134(84)80016-1
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journal_title：Journal of inorganic biochemistry
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doi：10.1016/j.jinorgbio.2018.02.018
更新日期：2018-06-01 00:00:00
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journal_title：Journal of inorganic biochemistry
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doi：10.1016/j.jinorgbio.2013.08.001
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journal_title：Journal of inorganic biochemistry
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journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
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更新日期：2008-09-01 00:00:00
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journal_title：Journal of inorganic biochemistry
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更新日期：1999-09-30 00:00:00
abstract：:The biochemically important anion, peroxynitrite, is commonly thought to have a cis-conformation which is stable. This is thought to have a cyclic structure, which blocks the formation of the trans-conformation. Furthermore, it is often suggested that the latter structure isomerises to the far more stable nitrate ion....
journal_title：Journal of inorganic biochemistry
pub_type： 杂志文章
doi：10.1016/s0162-0134(00)00057-x
更新日期：2000-03-01 00:00:00
