Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme.
about
Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociationNitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamicsControl of nitric oxide dynamics by guanylate cyclase in its activated state.Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: implications for nitric oxide sensors.Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c.Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser.Following ligand migration pathways from picoseconds to milliseconds in type II truncated hemoglobin from Thermobifida fusca.On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis.Direct observation of ligand transfer and bond formation in cytochrome c oxidase by using mid-infrared chirped-pulse upconversion.Increase in peripheral blood flow due to extraocular direct irradiation of visible light in rats.Ultrafast anisotropic protein quake propagation after CO photodissociation in myoglobin.Observation of the cascaded atomic-to-global length scales driving protein motion.Time-resolved visible and infrared study of the cyano complexes of myoglobin and of hemoglobin I from Lucina pectinata.Myoglobin: the hydrogen atom of biology and a paradigm of complexityAltered ligand rebinding kinetics due to distal-side effects in hemoglobin chico (Lysbeta66(E10) --> thr).Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallographyUltrafast dynamics of diatomic ligand binding to nitrophorin 4.Coherent infrared emission from myoglobin crystals: an electric field measurement.Quaternary structure and geminate recombination in hemoglobin: flow-flash studies on alpha 2CO beta 2 and alpha 2 beta 2CO.Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: general regulatory implications for heme-based sensors.Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escapeDirect observations of ligand dynamics in hemoglobin by subpicosecond infrared spectroscopySpin-dependent mechanism for diatomic ligand binding to heme.Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Femtosecond stimulated Raman spectroscopy by six-wave mixing.Ultrafast ligand dynamics in the heme-based GAF sensor domains of the histidine kinases DosS and DosT from Mycobacterium tuberculosis.Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy.Local changes in arterial oxygen saturation induced by visible and near-infrared light radiation.Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy.NO binding kinetics in myoglobin investigated by picosecond Fe K-edge absorption spectroscopy.Nonexponential protein relaxation: dynamics of conformational change in myoglobin.Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin.Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations.Spectroscopic evidence for conformational relaxation in myoglobin.Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?Perspective: Two-dimensional resonance Raman spectroscopy.Direct observation of subpicosecond vibrational dynamics in photoexcited myoglobin.Two-dimensional resonance Raman spectroscopy of oxygen- and water-ligated myoglobins.Changes in the apparent quantum efficiency for photolysis of Hb(CO)1.Ligand dynamics in the photodissociation of carboxyhemoglobin by subpicosecond transient infrared spectroscopy
P2860
Q27702127-865A5756-A995-4FE5-9388-B53A834C1F27Q28396269-BB6D27B1-9148-4291-BF55-82F9C5F47B3BQ30328713-482E6A56-C5A2-42B5-8C94-65EE19EA21FCQ30352944-8D6EBCA4-3FAF-46FE-9F84-54BDA50248E3Q30358672-5B652CB1-961F-4A89-8ED4-F7E83C792C92Q30413655-B35D2C5C-1C69-4C2F-8192-AF48420002C0Q30419154-3050605E-38FD-4C55-BD95-0B2BB8F4FF97Q30426850-52325DE7-809E-441A-B125-BF826202ACF8Q30480171-18B3E673-F795-42E8-AC9E-DCBFAA86204CQ30655204-4BC1138E-25F9-4669-8409-BD22B6A7EC60Q30814714-5CD94FE2-DFC4-4F1A-A5C0-ECB8A7544690Q30917961-ABC22C18-DDD5-46AD-9D4C-E1B7725A1251Q31109038-B71E6F66-D3B8-4BDA-880F-9818510883ADQ31149692-78CFC490-3471-4BF9-83E7-CA8D37138DC9Q33177688-DC756025-F23D-4338-AFFA-5B292049833BQ33607217-772F5FF4-02D9-4B3E-8DD2-80D1E6723686Q33716239-B267AE24-1C80-4BAB-B1F0-9F0A4EFBA43BQ34009163-225DF1F3-81C2-4D29-AC97-AC8A97CB04FFQ34091704-87580CED-0A75-4D2A-9A12-B240DAA06064Q34189716-3CCE93F2-1835-40F6-9761-313AFDE3C160Q34249185-9425B6F9-F62B-4DBF-B7C4-67BD792B4E46Q34316134-46E188C5-6A6A-4DDF-8E0A-F5A3B9408C6EQ34429772-EF6D6EB7-77C5-4C06-B424-42EBC7B74080Q34754684-FB47D164-5E90-45CA-9668-848F93D83F67Q35655344-A7A4F1EF-2BBA-48FA-A669-CD46A5D49F3DQ35663592-0B56CEFB-AE20-4D83-87A5-DF49D2F98FC5Q35778214-F644A572-C6B4-46CF-ADE3-05B9A1B2C673Q35861316-B7A8086F-1A48-48DB-BA47-DA4ACFF2EF0CQ35900999-C5CF34CC-0552-43ED-9F63-B06B63CAC9ABQ36207374-CAF1178D-3349-4403-A3D6-11C186614A87Q36376456-A7A0CFAB-DC26-4C49-B124-5885966070DAQ36598342-98F1629C-F306-478F-B2AA-0A8859B2B0D9Q36743967-20D167FB-49FE-4C9F-A688-685D08BD937BQ36927192-C21EF793-C773-42FC-9328-5EEE0C40DE55Q37108427-6F8C391A-70BC-43C5-8A70-239898E3CCA7Q38795166-FE64B259-715D-4441-AC35-6ABB74770DD0Q39164197-06EE9777-C525-4D8B-8674-CA6649A2ADA2Q39569282-9E5EFC45-5973-4403-992B-199744DA1DABQ39622534-F95D33B4-1459-42DA-A8A7-E39B4CB62708Q39624655-E7EB3D03-06A6-48CE-8758-DB2E00CE59BA
P2860
Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
1988年學術文章
@zh
1988年學術文章
@zh-hant
name
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@ast
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@en
type
label
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@ast
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@en
prefLabel
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@ast
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@en
P2093
P356
P1433
P1476
Photophysics and reactivity of ...... bin, myoglobin, and protoheme.
@en
P2093
P304
P356
10.1021/BI00411A022
P407
P577
1988-05-01T00:00:00Z