nitrogenase/karies gigi

Tautan disimpan ke clipboard

ArtikelUji klinisPaten

Pilih jenis pengurutan

Halaman 1 dari 26 hasil

Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Early studies in which nitrogenase was freeze-trapped during enzymatic turnover revealed the presence of high-spin ( S = 3/2) electron paramagnetic resonance (EPR) signals from the active-site FeMo-cofactor (FeMo-co) in electron-reduced intermediates of the MoFe protein. Historically denoted as 1b

The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Structures recently proposed for the FeMo-cofactor and P-cluster pair of the nitrogenase molybdenum-iron (MoFe)-protein from Azotobacter vinelandii have been crystallographically verified at 2.2 angstrom resolution. Significantly, no hexacoordinate sulfur atoms are observed in either type of metal

N2 fixation estimates in real-time by cavity ring-down laser absorption spectroscopy.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

The most common currency for estimating N(2) fixation is acetylene reduction to ethylene. Real-time estimates of nitrogen fixation are needed to close the global nitrogen budget and these remain a critical gap in both laboratory and field experiments. We present a new method for continuous real-time

Nitrogenases-A Tale of Carbon Atom(s).

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Named after its ability to catalyze the reduction of nitrogen to ammonia, nitrogenase has a surprising rapport with carbon-both through the interstitial carbide that resides in the central cavity of its cofactor and through its ability to catalyze the reductive carbon-carbon coupling of small carbon

Immunocytochemical localization of nitrogenase in bacteria symbiotically associated with Azolla spp.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

In situ immunogold labeling and transmission electron microscopy were used to detect nitrogenase in bacteria (bactobionts) symbiotically associated with leaf cavities of Azolla caroliniana and Azolla filiculoides. In A. caroliniana, the Fe protein of the nitrogenase complex was detected in a subset

A molecular pathway for the egress of ammonia produced by nitrogenase.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Nitrogenase converts N2 to NH3, at one face of an Fe-Mo-S cluster (FeMo-co) buried in the protein. Through exploration of cavities in the structures of nitrogenase proteins, a pathway for the egress of ammonia from its generation site to the external medium is proposed. This pathway is conserved in

Model Calculations Suggest that the Central Carbon in the FeMo-Cofactor of Nitrogenase Becomes Protonated in the Process of Nitrogen Fixation.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Nitrogen activation by nitrogenase is one of the most important enzymatic processes on earth. In spite of the determination of X-ray structures of increasingly higher resolution, the nitrogenase mechanism is still not understood. In the most recent X-ray structures it has been shown that a carbon

Electron microscopy of the Mo-Fe-protein from Azotobacter vinelandii nitrogenase.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

The quaternary structure of the Mo-Fe-protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo-Fe-protein has been proposed: two alpha subunits are displaced relative to two beta subunits along a twofold axis, so the molecule can be characterized

Time-Resolved EPR Study of H2 Reductive Elimination from the Photoexcited Nitrogenase Janus E4(4H) Intermediate.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Nitrogenase is activated for N2 reduction through the accumulation of four reducing equivalents at the active-site FeMo-cofactor (FeMo-co: Fe7S9MoC; homocitrate) to form the key Janus intermediate, denoted E4(4H), whose lowest-energy structure contains two [Fe-H-Fe] bridging hydrides and two protons

Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

N2 reduction by nitrogenase involves the accumulation of four reducing equivalents at the active site FeMo-cofactor to form a state with two [Fe-H-Fe] bridging hydrides (denoted E4(4H), the Janus intermediate), and we recently demonstrated that the enzyme is activated to cleave the N≡N triple bond

Reversible Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride State, the E(4)(4H) Janus Intermediate.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

We recently demonstrated that N2 reduction by nitrogenase involves the obligatory release of one H2 per N2 reduced. These studies focus on the E4(4H) "Janus intermediate", which has accumulated four reducing equivalents as two [Fe-H-Fe] bridging hydrides. E4(4H) is poised to bind and reduce N2

Binding modes for the first coupled electron and proton addition to FeMoco of nitrogenase.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

A combined broken-symmetry density functional and electrostatics approach has been used to model the one-electron reduced and protonated state of the iron-molybdenum cofactor active site of nitrogenase. The active site of the protein contains Fe, Mo, S, N, and O atoms, and many possible sites for

The Azolla-Anabaena azollae Relationship : XII. Nitrogenase Activity and Phycobiliproteins of the Endophyte as a Function of Leaf Age and Cell Type.

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Nitrogenase activity was measured in leaves along the main stem axes of Azolla pinnata R. Br. The activity was negligible in leaves of the apical region, rapidly increased to a maximum as leaves matured, and declined in aging leaves. In situ absorption and fluorescence emission spectra were obtained

Recognition of Rhodobacter sphaeroides by microcontact-imprinted poly(ethylene-co-vinyl alcohol).

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

The immobilization of cells or microorganisms is important for bioseparations, in bioreactors producing cellular metabolites, and as receptors for biosensing. Cell-imprinted polymers (CIPs) have been shown to have cavities with complementary shapes and also high affinities for the template cells or

NTP Toxicology and Carcinogenesis Studies of Molybdenum Trioxide (CAS No. 1313-27-5) in F344 Rats and B6C3F1 Mice (Inhalation Studies).

Hanya pengguna terdaftar yang dapat menerjemahkan artikel

Masuk daftar

Molybdenum is an essential element for the function of nitrogenase in plants and as a cofactor for enzymes including xanthine oxidoreductase, aldehyde oxidase, and sulfide oxidase in animals. Molybdenum trioxide is used primarily as an additive to steel and corrosion-resistant alloys. It is also

Sebelumnya
1
2
Lanjut

Bergabunglah dengan
halaman facebook kami

Herbal & Natural Medicine

Database tanaman obat terlengkap yang didukung oleh sains

Bekerja dalam 55 bahasa
Pengobatan herbal didukung oleh sains
Pengenalan herbal melalui gambar
Peta GPS interaktif - beri tag herba di lokasi (segera hadir)
Baca publikasi ilmiah yang terkait dengan pencarian Anda
Cari tanaman obat berdasarkan efeknya
Atur minat Anda dan ikuti perkembangan berita, uji klinis, dan paten

Ketikkan gejala atau penyakit dan baca tentang jamu yang mungkin membantu, ketik jamu dan lihat penyakit dan gejala yang digunakan untuk melawannya.
* Semua informasi didasarkan pada penelitian ilmiah yang dipublikasikan