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	Structural features of aluminium(III) complexes with bioligands in glutamate dehydrogenase reaction system - A review
	Yang, Xiaodi; Zhang, Qianqian; Li, Laifa; Shen, Renfang
刊名	JOURNAL OF INORGANIC BIOCHEMISTRY
	2007-09-01
卷号	101期号:9页码:1242-1250
关键词	structural speciation constitution configuration conformation Al(III) complexes
ISSN号	0162-0134
通讯作者	Yang, Xiaodi(yangxiaodi@njnu.edu.cn)
英文摘要	Aluminium(III) complexes are essential for understanding the toxicity, bioavailability and transport mechanisms of aluminium in environmental and biological systems. Since elucidation of the exact structures of these weakly coordinated systems is very difficult, the structures of Al(III) complexes in glutamate dehydrogenase reactions system were investigated recently from the following four aspects: (1) Constitutional studies: The keto-enol tautomerism of the complexes between aluminium(III) ion and alpha-ketoglutarate ligands in acidic aqueous solutions was studied. It is clearly demonstrated that Al(III) can promote the keto-enol tautomerization of alpha-ketoglutarate. (2) Configurational studies: Compared with L-Glu, the complex stability Of D-Glu-Al is stronger, especially for the tridentate species. The result was further supported by computational results in the molecular mechanics model with the UFF forcefield. It is implied that Al(III) complexation may favor the racemization from L- to D-amino acids. (3) Conformational studies: At biologically relevant pH and concentrations of Al(III) and NADH, Al(III) was found to increase the percentage of folded forms of NADH, which results in reducing the activity of the coenzyme NADH in the hollow-dehydroacnase reactions system. However, the conformations of NAD(+) and Al-NAD(+) are dependent upon the solvents and other ligands in the complexes. (4) Biological effects: The effects of Al(III) on the activity of the glutamate dehydrogenase-catalyzed reactions were studied by monitoring the differential-pulse polarography reduction current of NAD+. At the physiologically relevant pH values (pH 6.5 and 7.5), the activity of the GDH enzyme was strongly dependent on the concentration of the Al(III) in the assayed mixture solutions. (c) 2007 Published by Elsevier Inc.
收录类别	ISTP ; SCI
WOS关键词	ACIDIC AQUEOUS-SOLUTIONS ; CHEMICAL SPECIATION ; AL(III) COMPLEXES ; LANTHANIDE IONS ; ORGANIC-ACIDS ; CYCLE ENZYMES ; AMINO-ACIDS ; TOXICITY ; NMR ; METABOLISM
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry
WOS类目	Biochemistry & Molecular Biology ; Chemistry, Inorganic & Nuclear
语种	英语
出版者	ELSEVIER SCIENCE INC
WOS记录号	WOS:000249966200008
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2558630
专题	南京土壤研究所
通讯作者	Yang, Xiaodi
作者单位	1.Chinese Acad Sci, Inst Soil Sci, State Key Lab Soil & Sustainable Agr, Nanjing 210008, Peoples R China 2.Nanjing Normal Univ, Dept Environm Sci, Coll Chem & Environm Sci, Nanjing 210097, Peoples R China
推荐引用方式 GB/T 7714	Yang, Xiaodi,Zhang, Qianqian,Li, Laifa,et al. Structural features of aluminium(III) complexes with bioligands in glutamate dehydrogenase reaction system - A review[J]. JOURNAL OF INORGANIC BIOCHEMISTRY,2007,101(9):1242-1250.
APA	Yang, Xiaodi,Zhang, Qianqian,Li, Laifa,&Shen, Renfang.(2007).Structural features of aluminium(III) complexes with bioligands in glutamate dehydrogenase reaction system - A review.JOURNAL OF INORGANIC BIOCHEMISTRY,101(9),1242-1250.
MLA	Yang, Xiaodi,et al."Structural features of aluminium(III) complexes with bioligands in glutamate dehydrogenase reaction system - A review".JOURNAL OF INORGANIC BIOCHEMISTRY 101.9(2007):1242-1250.

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