{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T02:57:03Z","timestamp":1790045823462,"version":"4.0.1"},"reference-count":66,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2002,12,9]],"date-time":"2002-12-09T00:00:00Z","timestamp":1039392000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2003,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Leghemoglobins facilitate diffusion of oxygen through root tissue to a bacterial terminal oxidase in much the same way that myoglobin transports oxygen from blood to muscle cell mitochondria. Leghemoglobin serves an additional role as an oxygen scavenger to prevent inhibition of nitrogen fixation. For this purpose, the oxygen affinity of soybean leghemoglobin is 20\u2010fold greater than myoglobin, resulting from an 8\u2010fold faster association rate constant combined with a 3\u2010fold slower dissociation rate constant. Although the biochemical mechanism used by myoglobin to bind oxygen has been described in elegant detail, an explanation for the difference in affinity between these two structurally similar proteins is not obvious. The present work demonstrates that, despite their similar structures, leghemoglobin uses methods different from myoglobin to regulate ligand affinity. Oxygen and carbon monoxide binding to a comprehensive set of leghemoglobin distal heme pocket mutant proteins in comparison to their myoglobin counterparts has revealed some of these mechanisms. The \u201cdistal histidine\u201d provides a crucial hydrogen bond to stabilize oxygen in myoglobin but has little effect on bound oxygen in leghemoglobin and is retained mainly for reasons of protein stability and prevention of heme loss. Furthermore, soybean leghemoglobin uses an unusual combination of HisE7 and TyrB10 to sustain a weak stabilizing interaction with bound oxygen. Thus, the leghemoglobin distal heme pocket provides a much lower barrier to oxygen association than occurs in myoglobin and oxygen dissociation is regulated from the proximal heme pocket. Proteins 2003;50:239\u2013248. \u00a9 2002 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.10277","type":"journal-article","created":{"date-parts":[[2002,12,17]],"date-time":"2002-12-17T14:13:01Z","timestamp":1040134381000},"page":"239-248","source":"Crossref","is-referenced-by-count":52,"title":["Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin"],"prefix":"10.1002","volume":"50","author":[{"given":"Suman","family":"Kundu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark S.","family":"Hargrove","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2002,12,9]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)42483-6"},{"key":"e_1_2_7_3_2","volume-title":"The biology of nitrogen fixation","author":"Appleby C","year":"1974"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0898-8838(08)60154-3"},{"key":"e_1_2_7_5_2","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/S0021-9258(17)31228-0","article-title":"The kinetics of ligand binding to plant hemoglobins: structural implications","volume":"264","author":"Gibson QH","year":"1989","journal-title":"J Biol Chem"},{"key":"e_1_2_7_6_2","first-page":"365","article-title":"The origin and functions of hemoglobin in plants","volume":"76","author":"Appleby C","year":"1992","journal-title":"Sci Progr"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/228726a0"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsb0197-78"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi002165q"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00070a023"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.1002\/prot.10048"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1996.0833"},{"key":"e_1_2_7_13_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr00027a007"},{"key":"e_1_2_7_14_2","doi-asserted-by":"crossref","first-page":"20007","DOI":"10.1016\/S0021-9258(17)45475-5","article-title":"Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site\u2010directed mutagenesis and laser photolysis techniques","volume":"265","author":"Carver TE","year":"1990","journal-title":"J Biol Chem"},{"key":"e_1_2_7_15_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1569"},{"key":"e_1_2_7_16_2","doi-asserted-by":"publisher","DOI":"10.1007\/s007750050169"},{"key":"e_1_2_7_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)41955-7"},{"key":"e_1_2_7_18_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.4.1594"},{"key":"e_1_2_7_19_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi9812470"},{"key":"e_1_2_7_20_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2001.4731"},{"key":"e_1_2_7_21_2","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1016\/S0021-9258(18)33026-6","article-title":"Interactions of ligands with the distal glutamine in elephant myoglobin","volume":"258","author":"Bartnicki D","year":"1983","journal-title":"J Biol Chem"},{"key":"e_1_2_7_22_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1527"},{"key":"e_1_2_7_23_2","doi-asserted-by":"crossref","first-page":"14443","DOI":"10.1016\/S0021-9258(19)49732-9","article-title":"A novel site\u2010directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate","volume":"267","author":"Carver TE","year":"1992","journal-title":"J Biol Chem"},{"key":"e_1_2_7_24_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.0034"},{"key":"e_1_2_7_25_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00184a021"},{"key":"e_1_2_7_26_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00435a022"},{"key":"e_1_2_7_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)33063-6"},{"key":"e_1_2_7_28_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00574a030"},{"key":"e_1_2_7_29_2","doi-asserted-by":"crossref","first-page":"3843","DOI":"10.1016\/S0021-9258(18)32743-1","article-title":"Proton nuclear magnetic resonance study of the dynamic stability of the heme pocket of soybean leghemoglobin a","volume":"258","author":"Kong SB","year":"1983","journal-title":"J Biol Chem"},{"key":"e_1_2_7_30_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00506a022"},{"key":"e_1_2_7_31_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)77948-4"},{"key":"e_1_2_7_32_2","first-page":"602","article-title":"X\u2010ray study of leghemoglobin. 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