PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33415980-1	2021	The biological global carbon cycle is largely regulated through microbial nickel enzymes, including carbon monoxide dehydrogenase (CODH), acetyl coenzyme A synthase (ACS), and methyl coenzyme M reductase (MCR).	Nickel	74-80	acyl-CoA synthetase short chain family member 2	Homo sapiens	138-164	
19584250-1	2009	A dinuclear nickel complex with methyl and thiolate ligands, Ni(dadt(Et))Ni(Me)(SDmp) (2), has been synthesized as a dinuclear Ni(d)-Ni(p)-site model of acetyl-CoA synthase (ACS) (dadt(Et) is N,N"-diethyl-3,7-diazanonane-1,9-dithiolate; Dmp is 2,6-dimesitylphenyl).	Nickel	12-18	acyl-CoA synthetase short chain family member 2	Homo sapiens	174-177	
14735332-0	2004	Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates.	Nickel	84-90	acyl-CoA synthetase short chain family member 2	Homo sapiens	60-69	
11683635-1	2001	Acetogenic bacteria contain acetyl-CoA synthase (ACS), an enzyme with two distinct nickel-iron-sulfur active sites connected by a tunnel through which CO migrates.	Nickel	83-89	acyl-CoA synthetase short chain family member 2	Homo sapiens	28-47	
11683635-1	2001	Acetogenic bacteria contain acetyl-CoA synthase (ACS), an enzyme with two distinct nickel-iron-sulfur active sites connected by a tunnel through which CO migrates.	Nickel	83-89	acyl-CoA synthetase short chain family member 2	Homo sapiens	49-52	
10684606-5	2000	Then, CO is condensed with a methyl group and coenzyme A at cluster A, another nickel iron-sulfur cluster in the ACS subunit.	Nickel	79-85	acyl-CoA synthetase short chain family member 2	Homo sapiens	113-116	
12862445-3	2003	These results provide supporting evidence for a biological role for reduced nickel in ACS.	Nickel	76-82	acyl-CoA synthetase short chain family member 2	Homo sapiens	86-89	
11827525-2	2002	ACS contains an active site nickel iron-sulfur cluster that forms a paramagnetic adduct with CO, called the nickel iron carbon (NiFeC) species, which we have hypothesized to be a key intermediate in acetyl-CoA synthesis.	Nickel	28-34	acyl-CoA synthetase short chain family member 2	Homo sapiens	0-3	
33415980-1	2021	The biological global carbon cycle is largely regulated through microbial nickel enzymes, including carbon monoxide dehydrogenase (CODH), acetyl coenzyme A synthase (ACS), and methyl coenzyme M reductase (MCR).	Nickel	74-80	acyl-CoA synthetase short chain family member 2	Homo sapiens	166-169	
33415980-3	2021	We have established a mutant of nickel-substituted azurin as a scaffold upon which to develop protein-based models of enzymatic intermediates, including the organometallic states of ACS.	Nickel	32-38	acyl-CoA synthetase short chain family member 2	Homo sapiens	182-185	
33017144-3	2020	DFT calculations have been performed to investigate the ACS reaction mechanism starting from three different oxidation states (+2, +1, and 0) of Nip, the nickel proximal to [Fe4S4].	Nickel	154-160	acyl-CoA synthetase short chain family member 2	Homo sapiens	56-59	
30509471-1	2018	The chapter focuses on the methods involved in producing and characterizing two key nickel-iron-sulfur enzymes in the Wood-Ljungdahl pathway (WLP) of anaerobic conversion of carbon dioxide fixation into acetyl-CoA: carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS).	Nickel	84-90	acyl-CoA synthetase short chain family member 2	Homo sapiens	256-275	
30509471-1	2018	The chapter focuses on the methods involved in producing and characterizing two key nickel-iron-sulfur enzymes in the Wood-Ljungdahl pathway (WLP) of anaerobic conversion of carbon dioxide fixation into acetyl-CoA: carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS).	Nickel	84-90	acyl-CoA synthetase short chain family member 2	Homo sapiens	277-280	
23322089-0	2013	Functional conversion of nickel-containing metalloproteins via molecular design: from a truncated acetyl-coenzyme A synthase to a nickel superoxide dismutase.	Nickel	25-31	acyl-CoA synthetase short chain family member 2	Homo sapiens	98-124	
28675928-1	2017	The acetyl coenzyme A synthase (ACS) enzyme plays a central role in the metabolism of anaerobic bacteria and archaea, catalyzing the reversible synthesis of acetyl-CoA from CO and a methyl group through a series of nickel-based organometallic intermediates.	Nickel	215-221	acyl-CoA synthetase short chain family member 2	Homo sapiens	4-30	
28675928-1	2017	The acetyl coenzyme A synthase (ACS) enzyme plays a central role in the metabolism of anaerobic bacteria and archaea, catalyzing the reversible synthesis of acetyl-CoA from CO and a methyl group through a series of nickel-based organometallic intermediates.	Nickel	215-221	acyl-CoA synthetase short chain family member 2	Homo sapiens	32-35	
28675928-3	2017	In this work, we have developed a protein-based model for the NiP center of acetyl coenzyme A synthase using a nickel-substituted azurin protein (NiAz).	Nickel	111-117	acyl-CoA synthetase short chain family member 2	Homo sapiens	76-102	
28675928-4	2017	NiAz is the first model nickel protein system capable of accessing three (NiI/NiII/NiIII) distinct oxidation states within a physiological potential range in aqueous solution, a critical feature for achieving organometallic ACS activity, and binds CO and -CH3 groups with biologically relevant affinity.	Nickel	24-30	acyl-CoA synthetase short chain family member 2	Homo sapiens	224-227	
23322089-1	2013	Truncated acetyl-coenzyme A synthase (ACS) was successfully converted into functional nickel superoxide dismutase (Ni-SOD) by molecular design and the designed metalloproteins possess new spectroscopic, structural, and electrochemical characteristics required for catalyzing O(2)( -) disproportionation, and exhibit impressive Ni-SOD activity.	Nickel	86-92	acyl-CoA synthetase short chain family member 2	Homo sapiens	10-36	
23322089-1	2013	Truncated acetyl-coenzyme A synthase (ACS) was successfully converted into functional nickel superoxide dismutase (Ni-SOD) by molecular design and the designed metalloproteins possess new spectroscopic, structural, and electrochemical characteristics required for catalyzing O(2)( -) disproportionation, and exhibit impressive Ni-SOD activity.	Nickel	86-92	acyl-CoA synthetase short chain family member 2	Homo sapiens	38-41	
20507077-1	2010	The distal nickel site of acetyl-CoA synthase (Ni(d)-ACS) and reduced nickel superoxide dismutase (Ni-SOD) display similar square-planar Ni(II)N(2)S(2) coordination environments.	Nickel	11-17	acyl-CoA synthetase short chain family member 2	Homo sapiens	53-56	
21402216-1	2011	The nickel- and iron-containing enzyme acetyl-CoA synthase (ACS) catalyzes de novo synthesis as well as overall cleavage of acetyl-CoA in acetogens, various other anaerobic bacteria, methanogens, and other archaea.	Nickel	4-10	acyl-CoA synthetase short chain family member 2	Homo sapiens	39-58	
21402216-1	2011	The nickel- and iron-containing enzyme acetyl-CoA synthase (ACS) catalyzes de novo synthesis as well as overall cleavage of acetyl-CoA in acetogens, various other anaerobic bacteria, methanogens, and other archaea.	Nickel	4-10	acyl-CoA synthetase short chain family member 2	Homo sapiens	60-63	
20669901-3	2010	The active site of ACS is the A-cluster, which is an unusual nickel-iron-sulfur cluster.	Nickel	61-67	acyl-CoA synthetase short chain family member 2	Homo sapiens	19-22	
20507077-2	2010	One difference between these two sites, however, is that the nickel ion in Ni-SOD contains a mixed amine/amidate coordination motif while the Ni(d) site in Ni-ACS contains a bisamidate coordination motif.	Nickel	61-67	acyl-CoA synthetase short chain family member 2	Homo sapiens	159-162