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	Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii
	Bian, Shao-Min; Wang, Huang-Ping; Zhou, Hui-Na; Zhao, Ying; Zhao, Jian-Feng; Huang, Ju-Fu
刊名	Journal of integrative plant biology
	2007-03-01
卷号	49期号:3页码:336-342
关键词	Absorption spectra Azotobacter vinelandii Characterization by matrix-assisted laser desorption ionization time-of-flight (maldi-tof) Circular dichroism spectra and titration Heme-binding protein (hbp59) Mutant strain dj35 Purification
ISSN号	1672-9072
DOI	10.1111/j.1672-9072.2006.00372.x
通讯作者	Huang, ju-fu(jfhuang@ibcas.ac.cn)
英文摘要	A new protein, an approximately 59-kda monomer containing iron atoms, was first isolated from the mutant strain dj35 of azotobacter vinelandii lipmann. after analysis by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, the protein was identified as the product of a predicted gene. thus, the protein was tentatively called hbp59. its absorption spectra (abs) in the reduced state exhibited three peaks at 421, 517, and 556 nm and the maximal peak was shifted from 421 to 413 nm after exposure of hbp59 to air. the soret circular dichroism (cd) spectrum of hbp59 in the reduced state displayed four positive peaks at 364, 382, 406, and 418 nm and two negative peaks at 398 and 433 nm; the delta epsilon (cd extinction coefficient) values of these peaks were found to be 0.92, 0.58, 0.87, 0.72, -0.65 and -1.12 l/mol per cm, respectively. titration with heme showed that the protein has 0.1 heme molecules/protein molecule. after hbp59 had fully interacted with heme, its maximal abs value and soret cd intensity were increased by approximately 10-fold compared with values before interaction. therefore, it seems that one molecule of hbp59 can be interacted with only one heme. these results indicate that hbp59 contains heme with low spin and may be involved in heme utilization or adhesion.
WOS关键词	CYTOCHROME-C BIOGENESIS ; NITROGEN-FIXATION ; MOFE PROTEIN ; RHIZOBIUM-LEGUMINOSARUM ; ESCHERICHIA-COLI ; CYCHJKL GENES ; IRON ; BACTERIOFERRITIN ; PRODUCTS ; NIFE
WOS研究方向	Biochemistry & Molecular Biology ; Plant Sciences
WOS类目	Biochemistry & Molecular Biology ; Plant Sciences
语种	英语
出版者	BLACKWELL PUBLISHING
WOS记录号	WOS:000244645200009
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2380336
专题	中国科学院大学
通讯作者	Huang, Ju-Fu
作者单位	1.Chinese Acad Sci, Key Lab Photosynthesis & Environm Mol Physiol, Inst Bot, Beijing 100093, Peoples R China 2.Fujian Normal Univ, Bioengn Coll, Beijing 350007, Peoples R China 3.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Bian, Shao-Min,Wang, Huang-Ping,Zhou, Hui-Na,et al. Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii[J]. Journal of integrative plant biology,2007,49(3):336-342.
APA	Bian, Shao-Min,Wang, Huang-Ping,Zhou, Hui-Na,Zhao, Ying,Zhao, Jian-Feng,&Huang, Ju-Fu.(2007).Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii.Journal of integrative plant biology,49(3),336-342.
MLA	Bian, Shao-Min,et al."Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii".Journal of integrative plant biology 49.3(2007):336-342.

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