myalgia 发表于 2025-3-28 15:36:26

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合唱队 发表于 2025-3-28 20:48:05

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LAITY 发表于 2025-3-28 23:05:19

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名字的误用 发表于 2025-3-29 03:45:27

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Matrimony 发表于 2025-3-29 08:21:30

Purification of Nitrogenase Proteinshods that have been developed over the past few decades chiefly for the purification of naturally expressed nitrogenase in the diazotroph .. In addition, purification and Fe-S reconstitution strategies are also outlined for the heterologously expressed nitrogenase proteins in ..

Confirm 发表于 2025-3-29 14:39:13

Reconstitution of Molybdoenzymes with Bis-Molybdopterin Guanine Dinucleotide Cofactorsl molybdoenzymes from different organisms. The assay has been further developed since then by using specific molybdenum enzymes as the source of Moco for the reconstitution of diverse purified apo-molybdoenzymes. Alternatively, the molybdenum cofactor can be synthesized in vitro from stable intermed

品牌 发表于 2025-3-29 18:53:44

Crystallization of Nitrogenase ProteinsXRD) methods has provided detailed atomic insights into the enzyme system and, in particular, its active site FeMo-cofactor. The following chapter outlines the general protocols for the crystallization of . (.) nitrogenase component proteins, with a special emphasis on different applications, such a

得意人 发表于 2025-3-29 20:03:19

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六个才偏离 发表于 2025-3-30 00:08:09

Chemical Synthesis of an Asymmetric Mimic of the Nitrogenase Active Siteimportant achievements in synthetic M-S chemistry, as this cluster catalyzes the reduction of C.-substrates in a similar manner to the extracted M-cluster. Even though the synthetic protocol for this cluster has been described in the literature, there are plenty of pitfalls for researchers unfamilia

ingenue 发表于 2025-3-30 07:04:13

1064-3745 alloprotein research and wants to address the unanswered mechanistic and biosynthetic questions of these fascinating enzyme systems..978-1-4939-9403-8978-1-4939-8864-8Series ISSN 1064-3745 Series E-ISSN 1940-6029
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查看完整版本: Titlebook: Metalloproteins; Methods and Protocol Yilin Hu Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019 Nitrogenase.Nit