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| Characterization of a FeMo cofactor-deficient MoFe protein from a nifE-deleted strain （DJ35） of Azotobacter vinelandii | |
| 作者姓名： | ZHAO Ying BIAN Shaomin ZHANG Chunxi ZHOU Huina WANG Huangping ZHAO Jianfeng HUANG Jufu |
| 作者单位： | [1]Key Laboratory of Photosynthesis and Environmental MolecuIar Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China [2]Graduate School, Chinese Academy of Sciences, Beijing 100039, China [3]Key Laboratory of Photochemistry, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China [4]Bioengineering College, Fujian Normal University, Fuzhou 360007, China |
| 摘 要： | A MoFe protein （△nifE Av1） with a purity of ～80% was purified from a nifE-deleted mutant of Azotobacter vinelandii DJ35. Compared with MoFe protein purified from wild-type strain OP （OP Av1）, △nifE Av1 had the same subunits composition, and had immune reaction with antibody to OP Av1, but its relative mobility in anaerobic native polyacrylamide gel electrophoresis （PAGE） was a little larger than that of OP Av1. Metal analysis showed that Mo and Fe contents of △nifE Av1 both apparently decreased. When complemented with OP Fe protein, △nifE Av1 had no C2H2-reduction activity, but it could be in vitro activated by FeMoco extracted from OP Av1. The circular dichroism （CD） spectrum of △nifE Av1 at ～450 nm was similar to that of OP Av1, while the EPR signal at g≈3.7 was absolutely silent, and the signal intensities at g≈4.3 and 2.0 decreased by 75% and 50%, respectively. The results indicated that △nifE Av1 purified from DJ35 was a FeMoco-deficient but P-cluster-containing MoFe protein. |
| 关 键 词： | MoFe蛋白质 固氮细菌 纯净度 ERP 厌氧性 |
| 收稿时间： | 2005-05-23 |
| 修稿时间： | 2005-05-232005-07-26 |
Characterization of a FeMo cofactor-deficient MoFe protein from anifE-deleted strain (DJ35) ofAzotobacter vinelandii |
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| ZHAO Ying BIAN Shaomin ZHANG Chunxi ZHOU Huina WANG Huangping ZHAO Jianfeng HUANG Jufu.Characterization of a FeMo cofactor-deficient MoFe protein from anifE-deleted strain (DJ35) ofAzotobacter vinelandii[J].Chinese Science Bulletin,2005,50(20):2305-2310. | |
| Authors: | Ying Zhao Shaomin Bian Chunxi Zhang Huina Zhou Huangping Wang Jianfeng Zhao Jufu Huang |
| Institution: | 1. Key Laboratory of Photosynthesis and Environmental Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, 100093, Beijing, China 2. Graduate School, Chinese Academy of Sciences, 100039, Beijing, China 3. Key Laboratory of Photochemistry, Institute of Chemistry, Chinese Academy of Sciences, 100080, Beijing, China 4. Bioengineering College, Fujian Normal University, 360007, Fuzhou, China |
| Abstract: | A MoFe protein (ΔnifE Avl) with a purity of ～80% was purified from a nifE-deleted mutant ofAzotobacter vinelandii DJ35. Compared with MoFe protein purified from wild-type strain OP (OP Av1), ΔnifE Av1 had the same subunits composition, and had immune reaction with antibody to OP Av1, but its relative mobility in anaerobic native polyacrylamide gel electrophoresis (PAGE) was a little larger than that of OP Av1. Metal analysis showed that Mo and Fe contents of ΔnifE Av1 both apparently decreased. When complemented with OP Fe protein, ΔnifE Av1 had no C2H2-reduction activity, but it could bein vitro activated by FeMoco extracted from OP Av1. The circular dichroism (CD) spectrum of ΔnifE Av1 at ～450 nm was similar to that of OP Av1, while the EPR signal at g～3.7 was absolutely silent, and the signal intensities at g～=4.3 and 2.0 decreased by 75% and 50%, respectively. The results indicated that ΔnifE Av1 purified from DJ35 was a FeMoco-deficient but P-cluster-containing MoFe protein. |
| Keywords: | Azotobacter vinelandii AnifE Av1 FeMoco P-cluster EPR |
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